M00123
type: Enzyme
active site residues resources: Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
active site residues resources: Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.
active site residues resources: Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.
active site residues resources: Bivalency as a principle for proteasome inhibition.
active site residues resources: Atomic force microscopy reveals two conformations of the 20 S proteasome from fission yeast.
active site residues resources: Opening doors into the proteasome.
active site residues resources: Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.
cath: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
ec: https://purl.uniprot.org/enzyme/3.4.25.1
kegg enzyme: proteasome endopeptidase complex
kegg product: Protein
kegg product: Peptide
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
macie: M0177
pdb: 1fntA
pdb: 1fntO
pdb: 1g0uG
pdb: 1g0uU
pdb: 1g65G
pdb: 1g65U
pdb: 1jd22
pdb: 1jd2G
pdb: 1rypA
pdb: 1rypO
pdb: 1fntB
pdb: 1fntP
pdb: 1g0uA
pdb: 1g0uO
pdb: 1g65A
pdb: 1g65O
pdb: 1jd2A
pdb: 1jd2V
pdb: 1rypB
pdb: 1rypP
pdb: 1fntC
pdb: 1fntQ
pdb: 1g0uB
pdb: 1g0uP
pdb: 1g65B
pdb: 1g65P
pdb: 1jd2B
pdb: 1jd2W
pdb: 1rypC
pdb: 1rypQ
pdb: 1fntD
pdb: 1fntR
pdb: 1g0uC
pdb: 1g0uQ
pdb: 1g65C
pdb: 1g65Q
pdb: 1jd2C
pdb: 1jd2X
pdb: 1rypD
pdb: 1rypR
pdb: 1fntE
pdb: 1fntS
pdb: 1g0uD
pdb: 1g0uR
pdb: 1g65D
pdb: 1g65R
pdb: 1jd2D
pdb: 1jd2Y
pdb: 1rypE
pdb: 1rypS
pdb: 1fntF
pdb: 1fntT
pdb: 1g0uE
pdb: 1g0uS
pdb: 1g65E
pdb: 1g65S
pdb: 1jd2E
pdb: 1jd2Z
pdb: 1rypF
pdb: 1rypT
pdb: 1fntG
pdb: 1fntU
pdb: 1g0uF

Analogue
compound: Peptide
ligand het code: 95A
pdb: 1jd2H

Analogue
compound: Peptide
ligand het code: 95A
pdb: 1jd2O

IntermediateAnalogue
ligand het code: EPX
pdb: 1g65K

IntermediateAnalogue
ligand het code: EPX
pdb: 1g65Y

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.812-814

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.969

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.105-106

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.5, p.466-470

ReferenceForCatalyticMechanism
reference index: 14
reference section: Figure 4, p.1190-1191

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.3582

ReferenceForCatalyticMechanism
reference index: 18
reference section: p.10980-10981

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.2, p.1237-1238

ReferenceForCatalyticMechanism
reference index: 29
reference section: p.28-29

ReferenceForCatalyticMechanism
reference index: 35
reference section: p.34-36

Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.60.20.10

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

Biogenesis, structure and function of the yeast 20S proteasome.
type: BibliographicResource
authors:
  item: Chen P
  item: Hochstrasser M
journal: EMBO J
pages: 2620-30
published year: 1995
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/7781614

Structure and structure formation of the 20S proteasome.
type: BibliographicResource
authors:
  item: Schmidt M
  item: Schmidtke G
  item: Kloetzel PM
journal: Mol Biol Rep
pages: 103-12
published year: 1997
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/9228290

Structure of 20S proteasome from yeast at 2.4 A resolution.
type: BibliographicResource
authors:
  item: Groll M
  item: Ditzel L
  item: Lowe J
  item: Stock D
  item: Bochtler M
  item: Bartunik HD
  item: Huber R
journal: Nature
pages: 463-71
published year: 1997
volume: 386
references: http://www.ncbi.nlm.nih.gov/pubmed/9087403
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P40302
references: P23639
references: P21242
references: P23638
references: P32379
references: P21243
references: P40303
references: P23724
references: P22141
references: P25451
references: P30657
references: P30656
references: P38624
references: P25043
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Proteasomes: structure and biology.
type: BibliographicResource
authors:
  item: Tanaka K
journal: J Biochem (Tokyo)
pages: 195-204
published year: 1998
volume: 123
references: http://www.ncbi.nlm.nih.gov/pubmed/9538192

Conformational constraints for protein self-cleavage in the proteasome.
type: BibliographicResource
authors:
  item: Ditzel L
  item: Huber R
  item: Mann K
  item: Heinemeyer W
  item: Wolf DH
  item: Groll M
journal: J Mol Biol
pages: 1187-91
published year: 1998
volume: 279
references: http://www.ncbi.nlm.nih.gov/pubmed/9642094

Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.
type: BibliographicResource
authors:
  item: Loidl G
  item: Groll M
  item: Musiol HJ
  item: Ditzel L
  item: Huber R
  item: Moroder L
journal: Chem Biol
pages: 197-204
published year: 1999
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/10099130

Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly.
type: BibliographicResource
authors:
  item: Arendt CS
  item: Hochstrasser M
journal: EMBO J
pages: 3575-85
published year: 1999
volume: 18
references: http://www.ncbi.nlm.nih.gov/pubmed/10393174

The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study.
type: BibliographicResource
authors:
  item: Groll M
  item: Heinemeyer W
  item: Jager S
  item: Ullrich T
  item: Bochtler M
  item: Wolf DH
  item: Huber R
journal: Proc Natl Acad Sci U S A
pages: 10976-83
published year: 1999
volume: 96
references: http://www.ncbi.nlm.nih.gov/pubmed/10500111

Proteasomes of the yeast S. cerevisiae: genes, structure and functions.
type: BibliographicResource
authors:
  item: Hilt W
  item: Wolf DH
journal: Mol Biol Rep
pages: 3-10
published year: 1995
volume: 21
references: http://www.ncbi.nlm.nih.gov/pubmed/7565661

Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity of alpha,beta-epoxyketone proteasome inhibitors.
type: BibliographicResource
authors:
  item: Groll M
  item: Kim KB
  item: Kairies N
  item: Crews C
journal: J Am Chem Soc
pages: 1237-8
published year: 2000
volume: 122
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Conservation of substructures in proteins: interfaces of secondary structural elements in proteasomal subunits.
type: BibliographicResource
authors:
  item: Gille C
  item: Goede A
  item: Preissner R
  item: Rother K
  item: Frommel C
journal: J Mol Biol
pages: 1147-54
published year: 2000
volume: 299
references: http://www.ncbi.nlm.nih.gov/pubmed/10843865

A gated channel into the proteasome core particle.
type: BibliographicResource
authors:
  item: Groll M
  item: Bajorek M
  item: Kohler A
  item: Moroder L
  item: Rubin DM
  item: Huber R
  item: Glickman MH
  item: Finley D
journal: Nat Struct Biol
pages: 1062-7
published year: 2000
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/11062564
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structural basis for the activation of 20S proteasomes by 11S regulators.
type: BibliographicResource
authors:
  item: Whitby FG
  item: Masters EI
  item: Kramer L
  item: Knowlton JR
  item: Yao Y
  item: Wang CC
  item: Hill CP
journal: Nature
pages: 115-20
published year: 2000
volume: 408
references: http://www.ncbi.nlm.nih.gov/pubmed/11081519
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The substrate translocation channel of the proteasome.
type: BibliographicResource
authors:
  item: Kohler A
  item: Bajorek M
  item: Groll M
  item: Moroder L
  item: Rubin DM
  item: Huber R
  item: Glickman MH
  item: Finley D
journal: Biochimie
pages: 325-32
published year: 2001
volume: 83
references: http://www.ncbi.nlm.nih.gov/pubmed/11295493

Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor.
type: BibliographicResource
authors:
  item: Groll M
  item: Koguchi Y
  item: Huber R
  item: Kohno J
journal: J Mol Biol
pages: 543-8
published year: 2001
volume: 311
references: http://www.ncbi.nlm.nih.gov/pubmed/11493007
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The 11S regulators of 20S proteasome activity.
type: BibliographicResource
authors:
  item: Hill CP
  item: Masters EI
  item: Whitby FG
journal: Curr Top Microbiol Immunol
pages: 73-89
published year: 2002
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/12083009

The 20S proteasome.
type: BibliographicResource
authors:
  item: Zwickl P
journal: Curr Top Microbiol Immunol
pages: 23-41
published year: 2002
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/12083007

Structural features of archaebacterial and eukaryotic proteasomes.
type: BibliographicResource
authors:
  item: Koster AJ
  item: Walz J
  item: Lupas A
  item: Baumeister W
journal: Mol Biol Rep
pages: 11-20
published year: 1995
volume: 21
references: http://www.ncbi.nlm.nih.gov/pubmed/7565658

Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system.
type: BibliographicResource
authors:
  item: Dantuma NP
  item: Masucci MG
journal: FEBS Lett
pages: 22-6
published year: 2002
volume: 529
references: http://www.ncbi.nlm.nih.gov/pubmed/12354607

Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution.
type: BibliographicResource
authors:
  item: Unno M
  item: Mizushima T
  item: Morimoto Y
  item: Tomisugi Y
  item: Tanaka K
  item: Yasuoka N
  item: Tsukihara T
journal: J Biochem (Tokyo)
pages: 171-3
published year: 2002
volume: 131
references: http://www.ncbi.nlm.nih.gov/pubmed/11820928

Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings.
type: BibliographicResource
authors:
  item: Kisselev AF
  item: Kaganovich D
  item: Goldberg AL
journal: J Biol Chem
pages: 22260-70
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11927581

The structure of the mammalian 20S proteasome at 2.75 A resolution.
type: BibliographicResource
authors:
  item: Unno M
  item: Mizushima T
  item: Morimoto Y
  item: Tomisugi Y
  item: Tanaka K
  item: Yasuoka N
  item: Tsukihara T
journal: Structure (Camb)
pages: 609-18
published year: 2002
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/12015144

The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
type: BibliographicResource
authors:
  item: Forster A
  item: Whitby FG
  item: Hill CP
journal: EMBO J
pages: 4356-64
published year: 2003
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/12941688

Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach.
type: BibliographicResource
authors:
  item: Groll M
  item: Huber R
journal: Biochim Biophys Acta
pages: 33-44
published year: 2004
volume: 1695
references: http://www.ncbi.nlm.nih.gov/pubmed/15571807

Role of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes.
type: BibliographicResource
authors:
  item: Ramos PC
  item: Marques AJ
  item: London MK
  item: Dohmen RJ
journal: J Biol Chem
pages: 14323-30
published year: 2004
volume: 279
references: http://www.ncbi.nlm.nih.gov/pubmed/14722099

The axial channel of the 20S proteasome opens upon binding of the PA200 activator.
type: BibliographicResource
authors:
  item: Ortega J
  item: Heymann JB
  item: Kajava AV
  item: Ustrell V
  item: Rechsteiner M
  item: Steven AC
journal: J Mol Biol
pages: 1221-7
published year: 2005
volume: 346
references: http://www.ncbi.nlm.nih.gov/pubmed/15713476

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation.
type: BibliographicResource
authors:
  item: Brannigan JA
  item: Dodson G
  item: Duggleby HJ
  item: Moody PC
  item: Smith JL
  item: Tomchick DR
  item: Murzin AG
journal: Nature
pages: 416-9
published year: 1995
volume: 378
references: http://www.ncbi.nlm.nih.gov/pubmed/7477383

Functions of the proteasome: the lysis at the end of the tunnel.
type: BibliographicResource
authors:
  item: Goldberg AL
journal: Science
pages: 522-3
published year: 1995
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/7725095

Structure and functions of the 20S and 26S proteasomes.
type: BibliographicResource
authors:
  item: Coux O
  item: Tanaka K
  item: Goldberg AL
journal: Annu Rev Biochem
pages: 801-47
published year: 1996
volume: 65
references: http://www.ncbi.nlm.nih.gov/pubmed/8811196

Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly.
type: BibliographicResource
authors:
  item: Chen P
  item: Hochstrasser M
journal: Cell
pages: 961-72
published year: 1996
volume: 86
references: http://www.ncbi.nlm.nih.gov/pubmed/8808631

Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.
type: BibliographicResource
authors:
  item: Schmidtke G
  item: Kraft R
  item: Kostka S
  item: Henklein P
  item: Frommel C
  item: Lowe J
  item: Huber R
  item: Kloetzel PM
  item: Schmidt M
journal: EMBO J
pages: 6887-98
published year: 1996
volume: 15
references: http://www.ncbi.nlm.nih.gov/pubmed/9003765

Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.
type: BibliographicResource
authors:
  item: Arendt CS
  item: Hochstrasser M
journal: Proc Natl Acad Sci U S A
pages: 7156-61
published year: 1997
volume: 94
references: http://www.ncbi.nlm.nih.gov/pubmed/9207060

Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.
type: BibliographicResource
authors:
  item: Jager S
  item: Groll M
  item: Huber R
  item: Wolf DH
  item: Heinemeyer W
journal: J Mol Biol
pages: 997-1013
published year: 1999
volume: 291
references: http://www.ncbi.nlm.nih.gov/pubmed/10452902

Bivalency as a principle for proteasome inhibition.
type: BibliographicResource
authors:
  item: Loidl G
  item: Groll M
  item: Musiol HJ
  item: Huber R
  item: Moroder L
journal: Proc Natl Acad Sci U S A
pages: 5418-22
published year: 1999
volume: 96
references: http://www.ncbi.nlm.nih.gov/pubmed/10318898

Atomic force microscopy reveals two conformations of the 20 S proteasome from fission yeast.
type: BibliographicResource
authors:
  item: Osmulski PA
  item: Gaczynska M
journal: J Biol Chem
pages: 13171-4
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10747864

Opening doors into the proteasome.
type: BibliographicResource
authors:
  item: Pickart CM
  item: VanDemark AP
journal: Nat Struct Biol
pages: 999-1001
published year: 2000
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/11062549

Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.
type: BibliographicResource
authors:
  item: Ferrington DA
  item: Kapphahn RJ
journal: FEBS Lett
pages: 217-23
published year: 2004
volume: 578
references: http://www.ncbi.nlm.nih.gov/pubmed/15589823

Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
type: BibliographicResource
authors:
  item: Escherich A
  item: Ditzel L
  item: Musiol HJ
  item: Groll M
  item: Huber R
  item: Moroder L
journal: Biol Chem
pages: 893-8
published year: 1997
volume: 378
references: http://www.ncbi.nlm.nih.gov/pubmed/9377486

1fntH
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt

1fntI
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt

1fntL
type: Pdb
catalytic residue: THR 1;ASP 17; ;SER 131;ASP 168;SER 171
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt
comment: mutant K33R

1fntV
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt

1fntW
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt

1fntZ
type: Pdb
catalytic residue: THR 1;ASP 17; ;SER 131;ASP 168;SER 171
main chain in catalysis: THR 1;GLY 47
references: 1fnt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fnt
comment: mutant K33R

1g0u2
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g0uH
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g0uK
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g0uN
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g0uV
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g0uY
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g0u

1g652
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65

1g65H
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65

1g65K
type: Pdb
catalytic residue: ;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: ;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65
comment: complex with ligand (T1)

1g65N
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65

1g65V
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65

1g65Y
type: Pdb
catalytic residue: ;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: ;GLY 47
references: 1g65
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g65
comment: complex with ligand (T1)

1jd2H
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1jd2K
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1jd2N
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1jd2O
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1jd2R
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1jd2U
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1jd2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jd2

1rypH
type: Pdb
catalytic residue: ;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: ;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp
comment: mutant T1A

1rypI
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp

1rypL
type: Pdb
catalytic residue: THR 1;ASP 17; ;SER 131;ASP 168;SER 171
main chain in catalysis: THR 1;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp
comment: mutant K33R

1rypV
type: Pdb
catalytic residue: ;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: ;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp
comment: mutant T1A

1rypW
type: Pdb
catalytic residue: THR 1;ASP 17;LYS 33;SER 129;ASP 166;SER 169
main chain in catalysis: THR 1;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp

1rypZ
type: Pdb
catalytic residue: THR 1;ASP 17; ;SER 131;ASP 168;SER 171
main chain in catalysis: THR 1;GLY 47
references: 1ryp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ryp
comment: mutant K33R

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

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

ingensin
type: KeggEnzyme

macropain
type: KeggEnzyme

multicatalytic endopeptidase complex
type: KeggEnzyme

prosome
type: KeggEnzyme

multicatalytic proteinase (complex)
type: KeggEnzyme

MCP
type: KeggEnzyme

proteasome
type: KeggEnzyme

large multicatalytic protease
type: KeggEnzyme

multicatalytic proteinase
type: KeggEnzyme

proteasome organelle
type: KeggEnzyme

alkaline protease
type: KeggEnzyme

26S protease
type: KeggEnzyme

tricorn proteinase
type: KeggEnzyme

tricorn protease
type: KeggEnzyme