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5QC6

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 Residues20
Detailsbinding site for residue BCJ A 901
ChainResidue
ATRP26
AHIS164
AGLY165
APHE211
AHOH1004
AHOH1029
AHOH1063
AHOH1099
AHOH1100
BTYR118
BGLY119
AGLY62
BHOH1084
AGLY69
APHE70
AMET71
AGLY137
AASN161
AVAL162
AASN163

site_idAC2
Number of Residues23
Detailsbinding site for residue BCJ B 901
ChainResidue
ATYR118
BGLY62
BLYS64
BASN67
BGLY68
BGLY69
BPHE70
BMET71
BTHR73
BGLY137
BASN161
BVAL162
BASN163
BHIS164
BGLY165
BPHE211
BHOH1008
BHOH1021
BHOH1044
BHOH1055
BHOH1060
BHOH1114
BHOH1168

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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ASER25
AHIS164
AASN184
BSER25
BHIS164
BASN184

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 2024-10-30

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