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1U9X

Crystal Structure of the Cysteine Protease Human Cathepsin K in Complex with the Covalent Inhibitor NVP-ABJ688

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE IHJ A 300
ChainResidue
AGLN19
ACYS63
AGLY64
AGLY66
ATYR67
AALA134
AASN161
AHIS162
ALEU209
AHOH495
AGLY23
ASER24
ACYS25
ALYS40
ALYS41
ATHR42
AGLY43
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

220113

PDB entries from 2024-05-22

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