D00471
type: Enzyme
rlcp: p966
cath: Cathepsin D, subunit A; domain 1
ec: https://purl.uniprot.org/enzyme/3.4.23.16
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/2.7.7.7
ec: https://purl.uniprot.org/enzyme/3.1.26.4
csa: 1a30
csa: 1hiv
macie: M0175
uniprot: P03366
uniprot: P04585
uniprot: P04587
uniprot: P35963
kegg enzyme: HIV-1 retropepsin
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
kegg product: Protein
kegg product: Peptide
kegg intermediate: Amino-diol-tetrahedral intermediate
pdb: 1a30A
pdb: 1ajvA
pdb: 1ajxA
pdb: 1axaA
pdb: 1bdlA
pdb: 1bdqA
pdb: 1bdrA
pdb: 1bv7A
pdb: 1bv9A
pdb: 1bveA
pdb: 1bvgA
pdb: 1bwaA
pdb: 1bwbA
pdb: 1d4hA
pdb: 1d4iA
pdb: 1d4jA
pdb: 1dmpA
pdb: 1dw6C
pdb: 1ebkC
pdb: 1ebkE
pdb: 1ebwA
pdb: 1ebyA
pdb: 1ebzA
pdb: 1ec0A
pdb: 1ec1A
pdb: 1ec2A
pdb: 1ec3A
pdb: 1fejC
pdb: 1ff0C
pdb: 1fffC
pdb: 1ffiC
pdb: 1fg6C
pdb: 1fg8C
pdb: 1fgcC
pdb: 1g2kA
pdb: 1g6lA01
pdb: 1gnnA
pdb: 1gnoA
pdb: 1hbvA
pdb: 1hefE
pdb: 1hegE
pdb: 1hihA
pdb: 1hivA
pdb: 1hosA
pdb: 1hpsA
pdb: 1hpvA
pdb: 1hteA
pdb: 1htfA
pdb: 1htgA
pdb: 1hvhA
pdb: 1hviA
pdb: 1hvjA
pdb: 1hvkA
pdb: 1hvlA
pdb: 1hvrA
pdb: 1hvsA
pdb: 1hwrA
pdb: 1hxbA
pdb: 1k1tA

Cathepsin D, subunit A; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.70.10
catalytic domain: index.html

Protein
type: KeggSubstrate
references: KEGG:C00017
compound type: peptide/protein
type: KeggProduct

Peptide
type: KeggSubstrate
references: KEGG:C00012
compound type: peptide/protein
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Amino-diol-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00136

1a30A
type: Pdb
references: 1a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a30
catalytic residue: ASP 25

1ajvA
type: Pdb
references: 1ajv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ajv
catalytic residue: ASP 25

1ajxA
type: Pdb
references: 1ajx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ajx
catalytic residue: ASP 25

1axaA
type: Pdb
references: 1axa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1axa
catalytic residue: ASP 25
comment: mutant A28S

1bdlA
type: Pdb
references: 1bdl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdl
catalytic residue: ASP 25
comment: mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E

1bdqA
type: Pdb
references: 1bdq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdq
catalytic residue: ASP 25
comment: mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E, I47V, V82I

1bdrA
type: Pdb
references: 1bdr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdr
catalytic residue: ASP 25
comment: mutant T31S, L33V, E34T, E35G, M36I, S37E

1bv7A
type: Pdb
references: 1bv7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bv7
catalytic residue: ASP 25

1bv9A
type: Pdb
references: 1bv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bv9
catalytic residue: ASP 25
comment: mutant I84V

1bveA
type: Pdb
references: 1bve
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bve
catalytic residue: ASP 25
comment: mutant C95A

1bvgA
type: Pdb
references: 1bvg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvg
catalytic residue: ASP 25
comment: mutant C95A

1bwaA
type: Pdb
references: 1bwa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bwa
catalytic residue: ASP 25
comment: mutant V82F, I84V

1bwbA
type: Pdb
references: 1bwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bwb
catalytic residue: ASP 25
comment: mutant V82F, I84V

1d4hA
type: Pdb
references: 1d4h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4h
catalytic residue: ASP 25

1d4iA
type: Pdb
references: 1d4i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4i
catalytic residue: ASP 25

1d4jA
type: Pdb
references: 1d4j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4j
catalytic residue: ASP 25

1dmpA
type: Pdb
references: 1dmp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dmp
catalytic residue: ASP 25

1dw6C
type: Pdb
references: 1dw6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dw6
catalytic residue: ASP 25
comment: mutant Q7K, L33I, L63I, C67A, L90M, C95A

1ebkC
type: Pdb
references: 1ebk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebk
catalytic residue: ASP 25
comment: mutant Q7K, R8Q, L33I, L63I, C67A, C95A

1ebkE
type: Pdb
references: 1ebk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebk
catalytic residue: ASP 25
comment: mutant Q7K, R8Q, L33I, L63I, C67A, C95A

1ebwA
type: Pdb
references: 1ebw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebw
catalytic residue: ASP 25

1ebyA
type: Pdb
references: 1eby
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eby
catalytic residue: ASP 25

1ebzA
type: Pdb
references: 1ebz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebz
catalytic residue: ASP 25

1ec0A
type: Pdb
references: 1ec0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec0
catalytic residue: ASP 25

1ec1A
type: Pdb
references: 1ec1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec1
catalytic residue: ASP 25

1ec2A
type: Pdb
references: 1ec2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec2
catalytic residue: ASP 25

1ec3A
type: Pdb
references: 1ec3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec3
catalytic residue: ASP 25

1fejC
type: Pdb
references: 1fej
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fej
catalytic residue: ASP 25
comment: mutant L90M

1ff0C
type: Pdb
references: 1ff0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ff0
catalytic residue: ASP 25
comment: mutant K45I

1fffC
type: Pdb
references: 1fff
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fff
catalytic residue: ASP 25
comment: mutant D30N

1ffiC
type: Pdb
references: 1ffi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ffi
catalytic residue: ASP 25
comment: mutant D30N

1fg6C
type: Pdb
references: 1fg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fg6
catalytic residue: ASP 25
comment: mutant N88D

1fg8C
type: Pdb
references: 1fg8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fg8
catalytic residue: ASP 25
comment: mutant N88D

1fgcC
type: Pdb
references: 1fgc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fgc
catalytic residue: ASP 25

1g2kA
type: Pdb
references: 1g2k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g2k
catalytic residue: ASP 25

1g6lA01
type: Pdb
references: 1g6l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g6l
catalytic residue: ASP 25

1gnnA
type: Pdb
references: 1gnn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gnn
catalytic residue: ASP 25
comment: mutant V82N

1gnoA
type: Pdb
references: 1gno
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gno
catalytic residue: ASP 25

1hbvA
type: Pdb
references: 1hbv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hbv
catalytic residue: ASP 25

1hefE
type: Pdb
references: 1hef
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hef
catalytic residue: ASP 25

1hegE
type: Pdb
references: 1heg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1heg
catalytic residue: ASP 25

1hihA
type: Pdb
references: 1hih
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hih
catalytic residue: ASP 25

1hivA
type: Pdb
references: 1hiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hiv
catalytic residue: ASP 25

1hosA
type: Pdb
references: 1hos
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hos
catalytic residue: ASP 25

1hpsA
type: Pdb
references: 1hps
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hps
catalytic residue: ASP 25

1hpvA
type: Pdb
references: 1hpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpv
catalytic residue: ASP 25

1hteA
type: Pdb
references: 1hte
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hte
catalytic residue: ASP 25

1htfA
type: Pdb
references: 1htf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htf
catalytic residue: ASP 25

1htgA
type: Pdb
references: 1htg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htg
catalytic residue: ASP 25

1hvhA
type: Pdb
references: 1hvh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvh
catalytic residue: ASP 25

1hviA
type: Pdb
references: 1hvi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvi
catalytic residue: ASP 25

1hvjA
type: Pdb
references: 1hvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvj
catalytic residue: ASP 25

1hvkA
type: Pdb
references: 1hvk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvk
catalytic residue: ASP 25

1hvlA
type: Pdb
references: 1hvl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvl
catalytic residue: ASP 25

1hvrA
type: Pdb
references: 1hvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvr
catalytic residue: ASP 25

1hvsA
type: Pdb
references: 1hvs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvs
catalytic residue: ASP 25
comment: mutant V82A

1hwrA
type: Pdb
references: 1hwr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwr
catalytic residue: ASP 25

1hxbA
type: Pdb
references: 1hxb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hxb
catalytic residue: ASP 25

1k1tA
type: Pdb
references: 1k1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k1t
catalytic residue: ASP 25
comment: mutant K45I, V82S

1k1uA
type: Pdb
references: 1k1u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k1u
catalytic residue: ASP 25
comment: mutant K45I, L90M

1k2bA
type: Pdb
references: 1k2b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2b
catalytic residue: ASP 25
comment: mutant N88D, L90M

1k2cA
type: Pdb
references: 1k2c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2c
catalytic residue: ASP 25
comment: mutant D30N, V82S

1k6cA
type: Pdb
references: 1k6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6c
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6pA
type: Pdb
references: 1k6p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6p
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6tA
type: Pdb
references: 1k6t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6t
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6vA
type: Pdb
references: 1k6v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6v
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1lv1A01
type: Pdb
references: 1lv1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lv1
catalytic residue: ASP 25
comment: mutant C95M

1merA
type: Pdb
references: 1mer
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mer
catalytic residue: ASP 25
comment: mutant I84V

1mesA
type: Pdb
references: 1mes
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mes
catalytic residue: ASP 25
comment: mutant I84V

1metA
type: Pdb
references: 1met
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1met
catalytic residue: ASP 25
comment: mutant V82F

1meuA
type: Pdb
references: 1meu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1meu
catalytic residue: ASP 25
comment: mutant V82F, I84V

1odwA
type: Pdb
references: 1odw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1odw
catalytic residue: ASP 25

1odxA
type: Pdb
references: 1odx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1odx
catalytic residue: ASP 25
comment: mutant A71T, V82A

1odyA
type: Pdb
references: 1ody
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ody
catalytic residue: ASP 25

1qbrA
type: Pdb
references: 1qbr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbr
catalytic residue: ASP 25

1qbsA
type: Pdb
references: 1qbs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbs
catalytic residue: ASP 25

1qbtA
type: Pdb
references: 1qbt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbt
catalytic residue: ASP 25

1qbuA
type: Pdb
references: 1qbu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbu
catalytic residue: ASP 25

1sbgA
type: Pdb
references: 1sbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sbg
catalytic residue: ASP 25

1tcxA
type: Pdb
references: 1tcx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcx
catalytic residue: ASP 25
comment: mutant I32V, V47I, I82V

2bpvA
type: Pdb
references: 2bpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpv
catalytic residue: ASP 25

2bpwA
type: Pdb
references: 2bpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpw
catalytic residue: ASP 25

2bpxA
type: Pdb
references: 2bpx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpx
catalytic residue: ASP 25

2bpyA
type: Pdb
references: 2bpy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpy
catalytic residue: ASP 25

2bpzA
type: Pdb
references: 2bpz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpz
catalytic residue: ASP 25

3phvA
type: Pdb
references: 3phv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3phv
catalytic residue: ASP 25

3tlhA
type: Pdb
references: 3tlh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tlh
catalytic residue: ASP 25

9hvpA
type: Pdb
references: 9hvp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9hvp
catalytic residue: ASP 25

1a30B
type: Pdb
references: 1a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a30
catalytic residue: ASP 25

1ajvB
type: Pdb
references: 1ajv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ajv
catalytic residue: ASP 25

1ajxB
type: Pdb
references: 1ajx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ajx
catalytic residue: ASP 25

1axaB
type: Pdb
references: 1axa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1axa
catalytic residue: ASP 25
comment: mutant A28S

1bdlB
type: Pdb
references: 1bdl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdl
catalytic residue: ASP 25
comment: mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E

1bdqB
type: Pdb
references: 1bdq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdq
catalytic residue: ASP 25
comment: mutant T31S, V32I, L33V, E34A, E35G, M36I, S37E, I47V, V82I

1bdrB
type: Pdb
references: 1bdr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bdr
catalytic residue: ASP 25
comment: mutant T31S, L33V, E34T, E35G, M36I, S37E

1bv7B
type: Pdb
references: 1bv7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bv7
catalytic residue: ASP 25

1bv9B
type: Pdb
references: 1bv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bv9
catalytic residue: ASP 25
comment: mutant I84V

1bveB
type: Pdb
references: 1bve
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bve
catalytic residue: ASP 25
comment: mutant C95A

1bvgB
type: Pdb
references: 1bvg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvg
catalytic residue: ASP 25
comment: mutant C95A

1bwaB
type: Pdb
references: 1bwa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bwa
catalytic residue: ASP 25
comment: mutant V82F, I84V

1bwbB
type: Pdb
references: 1bwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bwb
catalytic residue: ASP 25
comment: mutant V82F, I84V

1d4hB
type: Pdb
references: 1d4h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4h
catalytic residue: ASP 125

1d4iB
type: Pdb
references: 1d4i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4i
catalytic residue: ASP 125

1d4jB
type: Pdb
references: 1d4j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4j
catalytic residue: ASP 125

1dmpB
type: Pdb
references: 1dmp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dmp
catalytic residue: ASP 25

1dw6D
type: Pdb
references: 1dw6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dw6
catalytic residue: ASP 125
comment: mutant Q107K, L133I, L163I, C167A, L190M, C195A

1ebkD
type: Pdb
references: 1ebk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebk
catalytic residue: ASP 125
comment: mutant Q107K, R108Q, L133I, L163I, C167A, C195A

1ebkF
type: Pdb
references: 1ebk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebk
catalytic residue: ASP 125
comment: mutant Q107K, R108Q, L133I, L163I, C167A, C195A

1ebwB
type: Pdb
references: 1ebw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebw
catalytic residue: ASP 125

1ebyB
type: Pdb
references: 1eby
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eby
catalytic residue: ASP 125

1ebzB
type: Pdb
references: 1ebz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebz
catalytic residue: ASP 125

1ec0B
type: Pdb
references: 1ec0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec0
catalytic residue: ASP 125

1ec1B
type: Pdb
references: 1ec1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec1
catalytic residue: ASP 125

1ec2B
type: Pdb
references: 1ec2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec2
catalytic residue: ASP 125

1ec3B
type: Pdb
references: 1ec3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ec3
catalytic residue: ASP 125

1fejD
type: Pdb
references: 1fej
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fej
catalytic residue: ASP 125
comment: mutant L190M

1ff0D
type: Pdb
references: 1ff0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ff0
catalytic residue: ASP 125
comment: mutant K145I

1fffD
type: Pdb
references: 1fff
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fff
catalytic residue: ASP 125
comment: mutant D130N

1ffiD
type: Pdb
references: 1ffi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ffi
catalytic residue: ASP 125
comment: mutant D130N

1fg6D
type: Pdb
references: 1fg6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fg6
catalytic residue: ASP 125
comment: mutant N188D

1fg8D
type: Pdb
references: 1fg8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fg8
catalytic residue: ASP 125
comment: mutant N188D

1fgcD
type: Pdb
references: 1fgc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fgc
catalytic residue: ASP 125

1g2kB
type: Pdb
references: 1g2k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g2k
catalytic residue: ASP 25

1g6lA02
type: Pdb
references: 1g6l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g6l
catalytic residue: ASP 1025

1gnnB
type: Pdb
references: 1gnn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gnn
catalytic residue: ASP 25
comment: mutant V82N

1gnoB
type: Pdb
references: 1gno
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gno
catalytic residue: ASP 25

1hbvB
type: Pdb
references: 1hbv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hbv
catalytic residue: ASP 25

1hihB
type: Pdb
references: 1hih
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hih
catalytic residue: ASP 25

1hivB
type: Pdb
references: 1hiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hiv
catalytic residue: ASP 25

1hosB
type: Pdb
references: 1hos
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hos
catalytic residue: ASP 25

1hpsB
type: Pdb
references: 1hps
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hps
catalytic residue: ASP 25

1hpvB
type: Pdb
references: 1hpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpv
catalytic residue: ASP 25

1hteB
type: Pdb
references: 1hte
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hte
catalytic residue: ASP 25

1htfB
type: Pdb
references: 1htf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htf
catalytic residue: ASP 25

1htgB
type: Pdb
references: 1htg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htg
catalytic residue: ASP 25

1hvhB
type: Pdb
references: 1hvh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvh
catalytic residue: ASP 25

1hviB
type: Pdb
references: 1hvi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvi
catalytic residue: ASP 25

1hvjB
type: Pdb
references: 1hvj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvj
catalytic residue: ASP 25

1hvkB
type: Pdb
references: 1hvk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvk
catalytic residue: ASP 25

1hvlB
type: Pdb
references: 1hvl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvl
catalytic residue: ASP 25

1hvrB
type: Pdb
references: 1hvr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvr
catalytic residue: ASP 25

1hvsB
type: Pdb
references: 1hvs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hvs
catalytic residue: ASP 25
comment: mutant V82A

1hwrB
type: Pdb
references: 1hwr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hwr
catalytic residue: ASP 25

1hxbB
type: Pdb
references: 1hxb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hxb
catalytic residue: ASP 25

1k1tB
type: Pdb
references: 1k1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k1t
catalytic residue: ASP 125
comment: mutant K145I, V182S

1k1uB
type: Pdb
references: 1k1u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k1u
catalytic residue: ASP 125
comment: mutant K145I, L190M

1k2bB
type: Pdb
references: 1k2b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2b
catalytic residue: ASP 25
comment: mutant N88D, L90M

1k2cB
type: Pdb
references: 1k2c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2c
catalytic residue: ASP 25
comment: mutant D30N, V82S

1k6cB
type: Pdb
references: 1k6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6c
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6pB
type: Pdb
references: 1k6p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6p
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6tB
type: Pdb
references: 1k6t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6t
catalytic residue: ASP 25
comment: mutant Q7K, K14R, V82T, I84V

1k6vB
type: Pdb
references: 1k6v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k6v
catalytic residue: ASP 25
comment: mutant Q7K,K14R,V82T,I84V

1lv1A02
type: Pdb
references: 1lv1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lv1
catalytic residue: ASP 1025
comment: mutant C1095A

1merB
type: Pdb
references: 1mer
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mer
catalytic residue: ASP 25
comment: mutant I84V

1mesB
type: Pdb
references: 1mes
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mes
catalytic residue: ASP 25
comment: mutant I84V

1metB
type: Pdb
references: 1met
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1met
catalytic residue: ASP 25
comment: mutant V82F

1meuB
type: Pdb
references: 1meu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1meu
catalytic residue: ASP 25
comment: mutant V82F, I84V

1odwB
type: Pdb
references: 1odw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1odw
catalytic residue: ASP 25

1odxB
type: Pdb
references: 1odx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1odx
catalytic residue: ASP 25
comment: mutant A71T, V82A

1odyB
type: Pdb
references: 1ody
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ody
catalytic residue: ASP 25

1qbrB
type: Pdb
references: 1qbr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbr
catalytic residue: ASP 25

1qbsB
type: Pdb
references: 1qbs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbs
catalytic residue: ASP 25

1qbtB
type: Pdb
references: 1qbt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbt
catalytic residue: ASP 25

1qbuB
type: Pdb
references: 1qbu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbu
catalytic residue: ASP 25

1sbgB
type: Pdb
references: 1sbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sbg
catalytic residue: ASP 25

1tcxB
type: Pdb
references: 1tcx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tcx
catalytic residue: ASP 25
comment: mutant I32V, V47I, I82V

2bpvB
type: Pdb
references: 2bpv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpv
catalytic residue: ASP 25

2bpwB
type: Pdb
references: 2bpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpw
catalytic residue: ASP 25

2bpxB
type: Pdb
references: 2bpx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpx
catalytic residue: ASP 25

2bpyB
type: Pdb
references: 2bpy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpy
catalytic residue: ASP 25

2bpzB
type: Pdb
references: 2bpz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bpz
catalytic residue: ASP 25

9hvpB
type: Pdb
references: 9hvp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9hvp
catalytic residue: ASP 25

Analogue
compound: Peptide
pdb: 1a30A
ligand het code: GLU-ASP-LEU

Analogue
compound: Peptide
pdb: 1axaA
ligand het code: U0E-U0E

Analogue
compound: Peptide
pdb: 1bdqA
ligand het code: IM1

Analogue
compound: Peptide
pdb: 1bdrA
ligand het code: IM1

Analogue
compound: Peptide
pdb: 1dw6C
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLN

Analogue
compound: Peptide
pdb: 1ebkC
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLN

Analogue
compound: Peptide
pdb: 1ebkE
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLN

Analogue
compound: Peptide
pdb: 1fejC
ligand het code: ACE-THR-ILE-NLE-NLE-GLN-ARG

Analogue
compound: Peptide
pdb: 1ff0C
ligand het code: ACE-THR-ILE-NLE-NLE-GLN-ARG

Analogue
compound: Peptide
pdb: 1fffC
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2

Analogue
compound: Peptide
pdb: 1ffiC
ligand het code: ACE-THR-ILE-NLE-NLE-GLN-ARG

Analogue
compound: Peptide
pdb: 1fg6C
ligand het code: ACE-THR-ILE-NLE-NLE-GLN-ARG

Analogue
compound: Peptide
pdb: 1fg8C
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2

Analogue
compound: Peptide
pdb: 1fgcC
ligand het code: ACE-THR-ILE-NLE-NLE-GLN-ARG

Analogue
compound: Peptide
pdb: 1gnnA
ligand het code: U0E-U0E

Analogue
compound: Peptide
pdb: 1gnoA
ligand het code: U0E-U0E

Analogue
compound: Peptide
pdb: 1hbvA
ligand het code: GAN

Analogue
compound: Peptide
pdb: 1hefE
ligand het code: ALA-ALA-PHE-OHE-PHE-VAL-VAL-OME

Analogue
compound: Peptide
pdb: 1hegE
ligand het code: ALA-ALA-PHE-OHE-GLY-VAL-VAL-OME

Analogue
compound: Peptide
pdb: 1hihA
ligand het code: C20

Analogue
compound: Peptide
pdb: 1hivA
ligand het code: NOA-HIS-CAV-ILE-APY

Analogue
compound: Peptide
pdb: 1hpsA
ligand het code: RUN-RUN

Analogue
compound: Peptide
pdb: 1hpvA
ligand het code: 478

Analogue
compound: Peptide
pdb: 1htgA
ligand het code: G37

Analogue
compound: Peptide
pdb: 1hvjA
ligand het code: A78

Analogue
compound: Peptide
pdb: 1hxbA
ligand het code: QNC-ASN-HPH-DIQ-NTB

Analogue
compound: Peptide
pdb: 1k1tA
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE

Analogue
compound: Peptide
pdb: 1k1uA
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE

Analogue
compound: Peptide
pdb: 1k2bA
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2

Analogue
compound: Peptide
pdb: 1k2cA
ligand het code: ARG-VAL-DCL-PHE-GLU-ALA-NLE-NH2

Analogue
compound: Peptide
pdb: 1k6cA
ligand het code: MK1

Analogue
compound: Peptide
pdb: 1k6pA
ligand het code: XN3

Analogue
compound: Peptide
pdb: 1k6tA
ligand het code: XN1

Analogue
compound: Peptide
pdb: 1k6vA
ligand het code: XN2

Analogue
compound: Peptide
pdb: 1odwA
ligand het code: BOC-HPH-DMN-HPH-BOC

Analogue
compound: Peptide
pdb: 1odxA
ligand het code: BOC-HPH-DMN-HPH-BOC

Analogue
compound: Peptide
pdb: 1odyA
ligand het code: LP1

Analogue
compound: Peptide
pdb: 1sbgA
ligand het code: IM1

Analogue
compound: Peptide
pdb: 1tcxA
ligand het code: IM1

Analogue
compound: Peptide
pdb: 2bpvA
ligand het code: 1IN

Analogue
compound: Peptide
pdb: 2bpwA
ligand het code: 1IN

Analogue
compound: Peptide
pdb: 2bpxA
ligand het code: MK1

Analogue
compound: Peptide
pdb: 2bpyA
ligand het code: 3IN

Analogue
compound: Peptide
pdb: 2bpzA
ligand het code: 3IN

Analogue
compound: Peptide
pdb: 3tlhA
ligand het code: INT

Analogue
compound: Peptide
pdb: 9hvpA
ligand het code: PHQ-VAL-COR-VAL-PHQ

Analogue
compound: Protein
pdb: 1htfA
ligand het code: G26

Analogue
compound: Peptide
pdb: 1bdlA
ligand het code: IM1

Analogue
compound: Peptide
pdb: 1hteA
ligand het code: G23

Analogue
compound: Peptide
pdb: 1bdlB
ligand het code: IM1

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ajvA
ligand het code: NMB

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ajxA
ligand het code: AH1

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bv7A
ligand het code: XV6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bv9A
ligand het code: XV6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bveA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bvgA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bwaA
ligand het code: XV6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bwbA
ligand het code: 146

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1d4hA
ligand het code: BEH

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1d4iA
ligand het code: BEG

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1d4jA
ligand het code: MSC

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1dmpA
ligand het code: DMQ

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ebwA
ligand het code: BEI

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ebyA
ligand het code: BEB

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ebzA
ligand het code: BEC

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ec0A
ligand het code: BED

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ec1A
ligand het code: BEE

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ec2A
ligand het code: BEJ

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ec3A
ligand het code: MS3

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1g2kA
ligand het code: NM1

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hosA
ligand het code: PHP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hvhA
ligand het code: Q82

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hviA
ligand het code: A77

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hvkA
ligand het code: A79

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hvlA
ligand het code: A76

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hvrA
ligand het code: XK2

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hvsA
ligand het code: A77

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1hwrA
ligand het code: 216

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1merA
ligand het code: DMQ

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1mesA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1metA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1meuA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1qbrA
ligand het code: XV6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1qbsA
ligand het code: DMP

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1qbtA
ligand het code: 146

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1qbuA
ligand het code: 846

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.302

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.4, p.8461-8462

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.1607-1608

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.5, p.24363-24365

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.7978-7979

ReferenceForCatalyticMechanism
reference index: 33
reference section: Fig.7, p.12942-12943

ReferenceForCatalyticMechanism
reference index: 39
reference section: Fig.17, p.336-339

ReferenceForCatalyticMechanism
reference index: 40
reference section: p.949

ReferenceForCatalyticMechanism
reference index: 42
reference section: p.682

ReferenceForCatalyticMechanism
reference index: 79
reference section: Fig.8, p.803

ReferenceForCatalyticMechanism
reference index: 81
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 100
reference section: Fig.2

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Molecular dynamics of HIV-1 protease in complex with a difluoroketone-containing inhibitor: implications for the catalytic mechanism.
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Molecular modeling of the HIV-1 protease and its substrate binding site.
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Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution.
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Domain communication in the dynamical structure of human immunodeficiency virus 1 protease.
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Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease.
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The three-dimensional x-ray crystal structure of HIV-1 protease complexed with a hydroxyethylene inhibitor.
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Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism.
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Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
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Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S.
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Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere.
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comment: X-ray crystallography
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The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations.
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comment: X-ray crystallography
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Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling.
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Structure-based inhibitors of HIV-1 protease.
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Inhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate. Synthesis and crystallographic analysis.
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An orally bioavailable HIV-1 protease inhibitor containing an imidazole-derived peptide bond replacement: crystallographic and pharmacokinetic analysis.
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X-ray crystallographic studies of a series of penicillin-derived asymmetric inhibitors of HIV-1 protease.
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Influence of stereochemistry on activity and binding modes for C2 symmetry-based diol inhibitors of HIV-1 protease.
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Rational design, synthesis, and crystallographic analysis of a hydroxyethylene-based HIV-1 protease inhibitor containing a heterocyclic P1'--P2' amide bond isostere.
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Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors.
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X-ray structure of a tethered dimer for HIV-1 protease.
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Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming.
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Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme.
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comment: X-ray crystallography
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Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials.
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A check on rational drug design: crystal structure of a complex of human immunodeficiency virus type 1 protease with a novel gamma-turn mimetic inhibitor.
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comment: X-ray crystallography
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Flexibility and function in HIV-1 protease.
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journal: Nat Struct Biol
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Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
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Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
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comment: X-ray crystallography
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Regulation of HIV-1 protease activity through cysteine modification.
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Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases.
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Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity.
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comment: X-ray crystallography
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Three-dimensional structures of HIV-1 and SIV protease product complexes.
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journal: Biochemistry
volume: 35
pages: 12933-44
published year: 1996
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Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272.
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journal: Biochemistry
volume: 35
pages: 9945-50
published year: 1996
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Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450.
type: BibliographicResource
comment: X-ray crystallography
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journal: Chem Biol
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published year: 1996
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Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration.
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journal: J Biol Chem
volume: 271
pages: 5458-63
published year: 1996
authors:
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Cyclic HIV protease inhibitors: synthesis, conformational analysis, P2/P2' structure-activity relationship, and molecular recognition of cyclic ureas.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8784449
journal: J Med Chem
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published year: 1996
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Preparation and structure-activity relationship of novel P1/P1'-substituted cyclic urea-based human immunodeficiency virus type-1 protease inhibitors.
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journal: J Med Chem
volume: 39
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published year: 1996
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Inhibition and catalytic mechanism of HIV-1 aspartic protease.
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journal: J Mol Biol
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published year: 1996
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Ionization states of the catalytic residues in HIV-1 protease.
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journal: Nat Struct Biol
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pages: 946-50
published year: 1996
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journal: Pac Symp Biocomput
pages: 638-52
published year: 1996
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title: Empirical free energy calculations of human immunodeficiency virus type 1 protease crystallographic complexes. II. Knowledge-based ligand-protein interaction potentials applied to thermodynamic analysis of hydrophobic mutations.

Molecular mechanics calculations on HIV-1 protease with peptide substrates correlate with experimental data.
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journal: Protein Eng
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published year: 1996
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Structural Analysis of the Native and Drug-Resistant HIV-1 Proteinases Complexed with an Aminodiol Inhibitor.
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comment: X-ray crystallography
journal: Protein Pept Lett
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pages: 399-406
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Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.
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medline id: 97022126
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journal: Protein Sci
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Molecular basis of HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with cyclic urea inhibitors.
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comment: X-ray crystallography
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journal: Biochemistry
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Structure of HOE/BAY 793 complexed to human immunodeficiency virus (HIV-1) protease in two different crystal forms--structure/function relationship and influence of crystal packing.
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journal: Eur J Biochem
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pages: 313-22
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The active site of HIV-1 protease.
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journal: Med Res Rev
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Conformational selectivity of HIV-1 protease cleavage of X-Pro peptide bonds and its implications.
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journal: J Biol Chem
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pages: 15603-6
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Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9083478
journal: J Med Chem
volume: 40
pages: 898-902
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Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9003516
journal: J Med Chem
volume: 40
pages: 181-91
published year: 1997
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An orally bioavailable pyrrolinone inhibitor of HIV-1 protease: computational analysis and X-ray crystal structure of the enzyme complex.
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references: http://www.ncbi.nlm.nih.gov/pubmed/9258349
journal: J Med Chem
volume: 40
pages: 2440-4
published year: 1997
authors:
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Analysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 A data.
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journal: Proteins
volume: 27
pages: 184-94
published year: 1997
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Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9757136
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 1053-60
published year: 1998
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X-ray crystallographic studies of the structure-function relationships of HIV-1 protease.
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journal: Adv Exp Med Biol
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pages: 59-63
published year: 1998
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Counteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9790666
journal: Biochemistry
volume: 37
pages: 15042-9
published year: 1998
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Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9485357
journal: Biochemistry
volume: 37
pages: 2105-10
published year: 1998
authors:
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Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9692985
journal: Biochemistry
volume: 37
pages: 10928-36
published year: 1998
authors:
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Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?
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references: http://www.ncbi.nlm.nih.gov/pubmed/9860826
journal: Biochemistry
volume: 37
pages: 17137-44
published year: 1998
authors:
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A quantitative structure-activity relationship study on some sulfolanes and arylthiomethanes acting as HIV-1 protease inhibitors.
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journal: Bioorg Med Chem
volume: 6
pages: 2185-92
published year: 1998
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Structural studies of HIV-1 protease-inhibiting antibodies.
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journal: Gen Physiol Biophys
volume: 17 Suppl 1
pages: 3-6
published year: 1998
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Molecular recognition of cyclic urea HIV-1 protease inhibitors.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9575185
journal: J Biol Chem
volume: 273
pages: 12325-31
published year: 1998
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Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9554878
journal: J Med Chem
volume: 41
pages: 1446-55
published year: 1998
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Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9521105
journal: Protein Sci
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Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
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journal: Protein Sci
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Reaction path and free energy calculations of the transition between alternate conformations of HIV-1 protease.
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journal: Proteins
volume: 32
pages: 7-16
published year: 1998
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Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.
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comment: X-ray crystallography
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journal: Eur J Biochem
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pages: 238-45
published year: 1999
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Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.
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journal: J Biol Chem
volume: 274
pages: 23437-42
published year: 1999
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Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease.
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journal: J Med Chem
volume: 43
pages: 3495-504
published year: 2000
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Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10651036
journal: Proteins
volume: 38
pages: 29-40
published year: 2000
authors:
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Determining the 3D structure of HIV-1 protease.
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journal: Science
volume: 288
pages: 1590
published year: 2000
authors:
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NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride.
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journal: FEBS Lett
volume: 509
pages: 218-24
published year: 2001
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Synthesis and comparative molecular field analysis (CoMFA) of symmetric and nonsymmetric cyclic sulfamide HIV-1 protease inhibitors.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11170625
journal: J Med Chem
volume: 44
pages: 155-69
published year: 2001
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Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11340661
journal: Proteins
volume: 43
pages: 455-64
published year: 2001
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1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR.
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comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11170214
journal: Proteins
volume: 43
pages: 57-64
published year: 2001
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Structural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody.
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journal: Structure
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Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations.
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comment: X-ray crystallography
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journal: Biochem Biophys Res Commun
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N1-(4-methyl-2-pyridyl)-2,3,6-trimethoxybenzamide copper(II) complex as an inhibitor of human immunodeficiency virus 1 protease.
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journal: Biochem Pharmacol
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HIV-1 protease: characterization of a catalytically competent enzyme-substrate intermediate.
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journal: Biochemistry
volume: 41
pages: 1302-7
published year: 2002
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Molecular dynamics simulations of the first steps of the reaction catalyzed by HIV-1 protease.
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journal: Biophys J
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pages: 794-807
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journal: J Med Chem
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  item: Sedlacek J
  item: Fabry M
title: Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor.

Role of conformational fluctuations in the enzymatic reaction of HIV-1 protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12051929
journal: J Mol Biol
volume: 319
pages: 567-83
published year: 2002
authors:
  item: Piana S
  item: Carloni P
  item: Parrinello M

Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11771964
journal: J Mol Biol
volume: 315
pages: 21-52
published year: 2002
authors:
  item: Zoete V
  item: Michielin O
  item: Karplus M

A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11773409
journal: J Virol
volume: 76
pages: 1349-58
published year: 2002
authors:
  item: Yoshimura K
  item: Kato R
  item: Kavlick MF
  item: Nguyen A
  item: Maroun V
  item: Maeda K
  item: Hussain KA
  item: Ghosh AK
  item: Gulnik SV
  item: Erickson JW
  item: Mitsuya H

Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11790852
journal: Protein Sci
volume: 11
pages: 418-29
published year: 2002
authors:
  item: King NM
  item: Melnick L
  item: Prabu-Jeyabalan M
  item: Nalivaika EA
  item: Yang SS
  item: Gao Y
  item: Nie X
  item: Zepp C
  item: Heefner DL
  item: Schiffer CA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12237461
journal: Protein Sci
volume: 11
pages: 2393-402
published year: 2002
authors:
  item: Piana S
  item: Carloni P
  item: Rothlisberger U

Combining mutations in HIV-1 protease to understand mechanisms of resistance.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12012342
journal: Proteins
volume: 48
pages: 107-16
published year: 2002
authors:
  item: Mahalingam B
  item: Boross P
  item: Wang YF
  item: Louis JM
  item: Fischer CC
  item: Tozser J
  item: Harrison RW
  item: Weber IT
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12005435
journal: Structure
volume: 10
pages: 369-81
published year: 2002
authors:
  item: Prabu-Jeyabalan M
  item: Nalivaika E
  item: Schiffer CA

A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12534275
journal: Biochemistry
volume: 42
pages: 631-8
published year: 2003
authors:
  item: Muzammil S
  item: Ross P
  item: Freire E

Molecular dynamics study of the connection between flap closing and binding of fullerene-based inhibitors of the HIV-1 protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12564936
journal: Biochemistry
volume: 42
pages: 1326-33
published year: 2003
authors:
  item: Zhu Z
  item: Schuster DI
  item: Tuckerman ME

Improved prediction of HIV-1 protease-inhibitor binding energies by molecular dynamics simulations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12675950
journal: BMC Struct Biol
volume: 3
pages: 2
published year: 2003
authors:
  item: Jenwitheesuk E
  item: Samudrala R

NMR elucidation of early folding hierarchy in HIV-1 protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12644464
journal: J Biol Chem
volume: 278
pages: 19980-5
published year: 2003
authors:
  item: Bhavesh NS
  item: Sinha R
  item: Mohan PM
  item: Hosur RV

Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12933791
journal: J Biol Chem
volume: 278
pages: 43311-9
published year: 2003
authors:
  item: Ishima R
  item: Torchia DA
  item: Lynch SM
  item: Gronenborn AM
  item: Louis JM

Cooperative fluctuations of unliganded and substrate-bound HIV-1 protease: a structure-based analysis on a variety of conformations from crystallography and molecular dynamics simulations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12696052
journal: Proteins
volume: 51
pages: 409-22
published year: 2003
authors:
  item: Kurt N
  item: Scott WR
  item: Schiffer CA
  item: Haliloglu T

Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 3. The free energy contribution of structural water molecules in HIV-1 protease complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15317462
journal: J Med Chem
volume: 47
pages: 4507-16
published year: 2004
authors:
  item: Fornabaio M
  item: Spyrakis F
  item: Mozzarelli A
  item: Cozzini P
  item: Abraham DJ
  item: Kellogg GE

The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15184023
journal: J Mol Biol
volume: 340
pages: 67-79
published year: 2004
authors:
  item: Levy Y
  item: Caflisch A
  item: Onuchic JN
  item: Wolynes PG

High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15066436
journal: J Mol Biol
volume: 338
pages: 341-52
published year: 2004
authors:
  item: Tie Y
  item: Boross PI
  item: Wang YF
  item: Gaddis L
  item: Hussain AK
  item: Leshchenko S
  item: Ghosh AK
  item: Louis JM
  item: Harrison RW
  item: Weber IT

Crystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14990731
journal: J Virol
volume: 78
pages: 3123-32
published year: 2004
authors:
  item: Logsdon BC
  item: Vickrey JF
  item: Martin P
  item: Proteasa G
  item: Koepke JI
  item: Terlecky SR
  item: Wawrzak Z
  item: Winters MA
  item: Merigan TC
  item: Kovari LC

Inhibitor design by wrapping packing defects in HIV-1 proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15289598
journal: Proc Natl Acad Sci U S A
volume: 101
pages: 11640-5
published year: 2004
authors:
  item: Fernandez A
  item: Rogale K
  item: Scott R
  item: Scheraga HA

HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15044738
journal: Protein Sci
volume: 13
pages: 1108-23
published year: 2004
authors:
  item: Perryman AL
  item: Lin JH
  item: McCammon JA

The role of hydrogen bonding in the enzymatic reaction catalyzed by HIV-1 protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14739332
journal: Protein Sci
volume: 13
pages: 513-28
published year: 2004
authors:
  item: Trylska J
  item: Grochowski P
  item: McCammon JA

human immunodeficiency virus type 1 protease
type: KeggEnzyme

gag protease
type: KeggEnzyme

HIV aspartyl protease
type: KeggEnzyme

HIV proteinase
type: KeggEnzyme

retroproteinase
type: KeggEnzyme

HIV-1 protease
type: KeggEnzyme

HIV-2 protease
type: KeggEnzyme