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1AU3

CRYSTAL STRUCTURE OF THE CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT PYRROLIDINONE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE PCM A 300
ChainResidue
ASER4
AGLY65
AGLY66
ATYR67
AALA134
AALA137
ASER138
AGLN143
ASER146
ALYS147
AASN161
AGLN19
AHIS162
ATRP184
ALEU209
AGLY20
AGLY23
ASER24
ACYS25
ATRP26
AGLU59
AASP61

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSS
ChainResidueDetails
AGLN19-SER30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHAVLAVGYG
ChainResidueDetails
ALEU160-GLY170

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. HWIiKNSWgenWGnkGYIlM
ChainResidueDetails
AHIS177-MET196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS25
AHIS162
AASN182

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AASN182
ACYS25
AHIS162

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN19
ACYS25
AHIS162

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AASN182
AGLN19
AHIS162

219140

PDB entries from 2024-05-01

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