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1AYU

CRYSTAL STRUCTURE OF CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT SYMMETRIC BISCARBOHYDRAZIDE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE INA A 300
ChainResidue
ASER4
ATRP26
AGLU59
AASP61
AGLY65
AGLY66
ATYR67
AMET68
APHE144
ATYR145
ASER146
AASN18
ALYS147
AASN161
AHIS162
AALA163
AILE171
ATRP184
AGLN19
AGLY20
AGLN21
ACYS22
AGLY23
ASER24
ACYS25

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

222624

PDB entries from 2024-07-17

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