D00439
type: Enzyme
rlcp: p966
cath: Cathepsin D, subunit A; domain 1
ec: https://purl.uniprot.org/enzyme/3.4.23.20
csa: 1apt
uniprot: P00798
kegg enzyme: penicillopepsin
kegg enzyme: peptidase A
kegg enzyme: Penicillium janthinellum aspartic proteinase
kegg substrate: Peptide
kegg substrate: Protein
kegg substrate: Trypsinogen
kegg substrate: Casein
kegg substrate: H2O
kegg product: Peptide
kegg product: Protein
kegg product: Trypsin
kegg intermediate: Amino-diol-tetrahedral intermediate
pdb: 1aptE01
pdb: 1apuE01
pdb: 1apvE01
pdb: 1apwE01
pdb: 1bxoA01
pdb: 1bxqA01
pdb: 1ppkE01
pdb: 1pplE01
pdb: 1ppmE01
pdb: 1weaA01
pdb: 1webA01
pdb: 1wecA01
pdb: 1wedA01
pdb: 2weaA01
pdb: 2webA01
pdb: 2wecA01
pdb: 2wedA01
pdb: 3appA01
pdb: 1aptE02
pdb: 1apuE02
pdb: 1apvE02
pdb: 1apwE02
pdb: 1bxoA02
pdb: 1bxqA02
pdb: 1ppkE02
pdb: 1pplE02
pdb: 1ppmE02
pdb: 1weaA02
pdb: 1webA02
pdb: 1wecA02
pdb: 1wedA02
pdb: 2weaA02
pdb: 2webA02
pdb: 2wecA02
pdb: 2wedA02
pdb: 3appA02
active site residues resources: P00798
references: Amino acid sequence around the active site aspartic acid in penicillopepsin.
references: An X-ray crystallographic approach to enzyme structure and function.
references: Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
references: Structure and refinement of penicillopepsin at 1.8 A resolution.
references: Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution.
references: Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions.
references: Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin.
references: Inhibition of aspartic proteases by pepstatin and 3-methylstatine derivatives of pepstatin. Evidence for collected-substrate enzyme inhibition.
references: Molecular dynamics study of the structure and dynamics of a protein molecule in a crystalline ionic environment, Streptomyces griseus protease A.
references: X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
references: Modeling of globular proteins. A distance-based data search procedure for the construction of insertion/deletion regions and Pro----non-Pro mutations.
references: Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
references: Studies on the mechanism of action of penicillopepsin.
references: Mechanism and pathway of penicillopepsin-catalyzed transpeptidation and evidence for noncovalent trapping of amino acid and peptide intermediates.
references: Refined structure of porcine pepsinogen at 1.8 A resolution.
references: Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.
references: Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
references: Crystallization and preliminary crystallographic characterization of aspartic proteinase-A from baker's yeast and its complexes with inhibitors.
references: Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.
references: Critical-point analysis in protein electron-density map interpretation.
references: Overcoming the unfavourable entropic contribution of ligand binding with a macrocyclic inhibitor bound to penicillopepsin.
references: Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
references: Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).
references: Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water.
comment: This enzyme belongs to the peptidase family-A1. This enzyme has got a catalytic dyad, composed of two aspartic acid residues, which is observed in other aspartate proteases, such as pepsin (D00436 in EzCatDB). It suggests that it may have a similar reaction mechanism.

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

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

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

Trypsinogen
type: KeggSubstrate
references: KEGG:L00076
compound type: peptide/protein

Casein
type: KeggSubstrate
references: KEGG:L00078
compound type: peptide/protein
compound type: phosphate group/phosphate ion

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

Trypsin
type: KeggProduct
references: KEGG:C00298
compound type: peptide/protein

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

1aptE01
type: Pdb
references: 1apt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apt
catalytic residue: ASP 33

1apuE01
type: Pdb
references: 1apu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apu
catalytic residue: ASP 33

1apvE01
type: Pdb
references: 1apv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apv
catalytic residue: ASP 33

1apwE01
type: Pdb
references: 1apw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apw
catalytic residue: ASP 33

1bxoA01
type: Pdb
references: 1bxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bxo
catalytic residue: ASP 33

1bxqA01
type: Pdb
references: 1bxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bxq
catalytic residue: ASP 33

1ppkE01
type: Pdb
references: 1ppk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppk
catalytic residue: ASP 33

1pplE01
type: Pdb
references: 1ppl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppl
catalytic residue: ASP 33

1ppmE01
type: Pdb
references: 1ppm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppm
catalytic residue: ASP 33

1weaA01
type: Pdb
references: 1wea
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wea
catalytic residue: ASP 33

1webA01
type: Pdb
references: 1web
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1web
catalytic residue: ASP 33

1wecA01
type: Pdb
references: 1wec
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wec
catalytic residue: ASP 33

1wedA01
type: Pdb
references: 1wed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wed
catalytic residue: ASP 33

2weaA01
type: Pdb
references: 2wea
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wea
catalytic residue: ASP 33

2webA01
type: Pdb
references: 2web
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2web
catalytic residue: ASP 33

2wecA01
type: Pdb
references: 2wec
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wec
catalytic residue: ASP 33

2wedA01
type: Pdb
references: 2wed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wed
catalytic residue: ASP 33

3appA01
type: Pdb
references: 3app
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3app
catalytic residue: ASP 33

1aptE02
type: Pdb
references: 1apt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apt
catalytic residue: ASP 213

1apuE02
type: Pdb
references: 1apu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apu
catalytic residue: ASP 213

1apvE02
type: Pdb
references: 1apv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apv
catalytic residue: ASP 213

1apwE02
type: Pdb
references: 1apw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1apw
catalytic residue: ASP 213

1bxoA02
type: Pdb
references: 1bxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bxo
catalytic residue: ASP 213

1bxqA02
type: Pdb
references: 1bxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bxq
catalytic residue: ASP 213

1ppkE02
type: Pdb
references: 1ppk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppk
catalytic residue: ASP 213

1pplE02
type: Pdb
references: 1ppl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppl
catalytic residue: ASP 213

1ppmE02
type: Pdb
references: 1ppm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ppm
catalytic residue: ASP 213

1weaA02
type: Pdb
references: 1wea
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wea
catalytic residue: ASP 213

1webA02
type: Pdb
references: 1web
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1web
catalytic residue: ASP 213

1wecA02
type: Pdb
references: 1wec
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wec
catalytic residue: ASP 213

1wedA02
type: Pdb
references: 1wed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wed
catalytic residue: ASP 213

2weaA02
type: Pdb
references: 2wea
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wea
catalytic residue: ASP 213

2webA02
type: Pdb
references: 2web
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2web
catalytic residue: ASP 213

2wecA02
type: Pdb
references: 2wec
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wec
catalytic residue: ASP 213

2wedA02
type: Pdb
references: 2wed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2wed
catalytic residue: ASP 213

3appA02
type: Pdb
references: 3app
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3app
catalytic residue: ASP 213

Amino acid sequence around the active site aspartic acid in penicillopepsin.
type: BibliographicResource
comment: ACTIVE SITE.
medline id: 71018406
references: http://www.ncbi.nlm.nih.gov/pubmed/5475460
journal: Can J Biochem
volume: 48
pages: 1014-6
published year: 1970
authors:
  item: Sodek J
  item: Hofmann T
references: P00798

An X-ray crystallographic approach to enzyme structure and function.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6769571
journal: Can J Biochem
volume: 58
pages: 252-71
published year: 1980
authors:
  item: James MN

Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6755464
journal: Proc Natl Acad Sci U S A
volume: 79
pages: 6137-41
published year: 1982
authors:
  item: James MN
  item: Sielecki A
  item: Salituro F
  item: Rich DH
  item: Hofmann T

Structure and refinement of penicillopepsin at 1.8 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/6341600
journal: J Mol Biol
volume: 163
pages: 299-361
published year: 1983
authors:
  item: James MN
  item: Sielecki AR
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution.
type: BibliographicResource
comment: X-ray crystallography (ISBN: 0935940022)
journal: Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium
volume: 1
pages: 521-30
published year: 1983
authors:
  item: James MNG
  item: Sielecki AR
  item: Moult J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3912235
journal: Biochem Soc Trans
volume: 13
pages: 1044-6
published year: 1985
authors:
  item: Blum M
  item: Cunningham A
  item: Bendiner M
  item: Hofmann T

Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3899173
journal: Biochemistry
volume: 24
pages: 3701-13
published year: 1985
authors:
  item: James MN
  item: Sielecki AR

Inhibition of aspartic proteases by pepstatin and 3-methylstatine derivatives of pepstatin. Evidence for collected-substrate enzyme inhibition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3927973
journal: Biochemistry
volume: 24
pages: 3165-73
published year: 1985
authors:
  item: Rich DH
  item: Bernatowicz MS
  item: Agarwal NS
  item: Kawai M
  item: Salituro FG
  item: Schmidt PG

Molecular dynamics study of the structure and dynamics of a protein molecule in a crystalline ionic environment, Streptomyces griseus protease A.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2125469
journal: Biochemistry
volume: 29
pages: 8658-76
published year: 1990
authors:
  item: Avbelj F
  item: Moult J
  item: Kitson DH
  item: James MN
  item: Hagler AT

X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2115088
journal: J Mol Biol
volume: 214
pages: 199-222
published year: 1990
authors:
  item: Cooper JB
  item: Khan G
  item: Taylor G
  item: Tickle IJ
  item: Blundell TL

Modeling of globular proteins. A distance-based data search procedure for the construction of insertion/deletion regions and Pro----non-Pro mutations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2266566
journal: J Mol Biol
volume: 216
pages: 991-1016
published year: 1990
authors:
  item: Summers NL
  item: Karplus M

Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2217165
journal: Proteins
volume: 8
pages: 62-81
published year: 1990
authors:
  item: Abad-Zapatero C
  item: Rydel TJ
  item: Erickson J

Studies on the mechanism of action of penicillopepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1812712
journal: Adv Exp Med Biol
volume: 306
pages: 243-54
published year: 1991
authors:
  item: Hofmann T
  item: Blum M
  item: Cunningham A

Mechanism and pathway of penicillopepsin-catalyzed transpeptidation and evidence for noncovalent trapping of amino acid and peptide intermediates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2033049
journal: J Biol Chem
volume: 266
pages: 9501-7
published year: 1991
authors:
  item: Blum M
  item: Cunningham A
  item: Pang H
  item: Hofmann T

Refined structure of porcine pepsinogen at 1.8 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2056534
journal: J Mol Biol
volume: 219
pages: 671-92
published year: 1991
authors:
  item: Sielecki AR
  item: Fujinaga M
  item: Read RJ
  item: James MN

Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1606144
journal: Biochemistry
volume: 31
pages: 5201-14
published year: 1992
authors:
  item: Fraser ME
  item: Strynadka NC
  item: Bartlett PA
  item: Hanson JE
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1567842
journal: Biochemistry
volume: 31
pages: 3872-86
published year: 1992
authors:
  item: James MN
  item: Sielecki AR
  item: Hayakawa K
  item: Gelb MH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallization and preliminary crystallographic characterization of aspartic proteinase-A from baker's yeast and its complexes with inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8345528
journal: J Mol Biol
volume: 232
pages: 701-3
published year: 1993
authors:
  item: Badasso M
  item: Wood SP
  item: Aguilar C
  item: Cooper JB
  item: Blundell TL
  item: Dreyer T

Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7932732
journal: J Mol Biol
volume: 243
pages: 100-15
published year: 1994
authors:
  item: Jiang JS
  item: Brunger AT

Critical-point analysis in protein electron-density map interpretation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9379922
journal: Methods Enzymol
volume: 277
pages: 131-57
published year: 1997
authors:
  item: Fortier S
  item: Chiverton A
  item: Glasgow J
  item: Leherte L

Overcoming the unfavourable entropic contribution of ligand binding with a macrocyclic inhibitor bound to penicillopepsin.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9561242
journal: Adv Exp Med Biol
volume: 436
pages: 355-9
published year: 1998
authors:
  item: Fraser ME
  item: Meyer JH
  item: Bartlett PA
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS).
medline id: 99055159
references: http://www.ncbi.nlm.nih.gov/pubmed/9836576
journal: Biochemistry
volume: 37
pages: 16839-45
published year: 1998
authors:
  item: Khan AR
  item: Parrish JC
  item: Fraser ME
  item: Smith WW
  item: Bartlett PA
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00798

Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10850809
journal: Protein Sci
volume: 9
pages: 991-1001
published year: 2000
authors:
  item: Cao QN
  item: Stubbs M
  item: Ngo KQ
  item: Ward M
  item: Cunningham A
  item: Pai EF
  item: Tu GC
  item: Hofmann T

Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12036355
journal: J Med Chem
volume: 45
pages: 2469-83
published year: 2002
authors:
  item: Cozzini P
  item: Fornabaio M
  item: Marabotti A
  item: Abraham DJ
  item: Kellogg GE
  item: Mozzarelli A

acid protease A
type: KeggEnzyme

Penicillium citrinum acid proteinase
type: KeggEnzyme

Penicillium cyclopium acid proteinase
type: KeggEnzyme

Penicillium expansum acid proteinase
type: KeggEnzyme

Penicillium janthinellum acid proteinase
type: KeggEnzyme

Penicillium expansum aspartic proteinase
type: KeggEnzyme

Penicillium aspartic proteinase
type: KeggEnzyme

Penicillium caseicolum aspartic proteinase
type: KeggEnzyme

Penicillium roqueforti acid proteinase
type: KeggEnzyme

Penicillium duponti aspartic proteinase
type: KeggEnzyme

Penicillium citrinum aspartic proteinase
type: KeggEnzyme

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1aptE01
ligand het code: IVA-VAL-VAL-LTA (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1apuE01
ligand het code: IVA-VAL-VAL-STA (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1apvE01
ligand het code: IVA-VAL-VAL-DFO-NME (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1apwE01
ligand het code: IVA-VAL-VAL-DFI-NME (chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bxoA01
ligand het code: PP7

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1bxqA01
ligand het code: PP8

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ppkE01
ligand het code: IVV

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1pplE01
ligand het code: 1Z7

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1ppmE01
ligand het code: 0P1

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1weaA01
ligand het code: PP6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1webA01
ligand het code: PP4

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1wecA01
ligand het code: PP5

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1wedA01
ligand het code: PP6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2weaA01
ligand het code: PP6

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2webA01
ligand het code: PP4

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2wecA01
ligand het code: PP5

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 2wedA01
ligand het code: PP6

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.13, p.3709-3711

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.3, p.5207

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.10, p.3883-3885