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5QC5

Crystal structure of human Cathepsin-S with bound ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue BAJ A 901
ChainResidue
ATRP26
AASN161
AVAL162
AASN163
AHIS164
AGLY165
APHE211
AHOH1006
AHOH1007
AHOH1032
AGLY62
ALYS64
AASN67
AGLY68
AGLY69
APHE70
AMET71
ATYR118

site_idAC2
Number of Residues20
Detailsbinding site for residue BAJ B 901
ChainResidue
BTRP26
BGLY62
BLYS64
BASN67
BGLY68
BGLY69
BPHE70
BMET71
BTYR118
BGLY137
BASN161
BVAL162
BASN163
BHIS164
BGLY165
BPHE211
BHOH1022
BHOH1024
BHOH1047
BHOH1069

Functional Information from PROSITE/UniProt
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHGVLVVGYG
ChainResidueDetails
AVAL162-GLY172

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWghnFGeeGYIrM
ChainResidueDetails
ATYR179-MET198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
AGLN19electrostatic stabiliser
ASER25nucleofuge, nucleophile, proton acceptor, proton donor
AHIS164proton acceptor, proton donor
AASN184electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
BGLN19electrostatic stabiliser
BSER25nucleofuge, nucleophile, proton acceptor, proton donor
BHIS164proton acceptor, proton donor
BASN184electrostatic stabiliser

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PDB entries from 2026-01-14

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