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5QBY

Crystal structure of human Cathepsin-S with bound ligand

Replaces:  3MPE
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 N2A A 901
ChainResidue
AASP6
APHE70
ATHR72
ATHR73
AGLU115
AVAL162
AHIS164
AGLY165
AGLU193
ATYR195
APHE211
AARG8
AHOH1130
AGLU9
ALYS60
AGLY62
ALYS64
AASN67
AGLY68
AGLY69

site_idAC2
Number of Residues19
Detailsbinding site for residue N2A B 901
ChainResidue
BASP6
BARG8
BGLU9
BLYS60
BGLY62
BLYS64
BASN67
BGLY68
BGLY69
BPHE70
BTHR73
BGLU115
BVAL162
BHIS164
BGLY165
BGLU193
BTYR195
BPHE211
BHOH1123

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 2024-07-24

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