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5QBV

Crystal structure of human Cathepsin-S with bound ligand

Replaces:  3MPF
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 Residues19
Detailsbinding site for residue N2D A 901
ChainResidue
AASP6
AMET71
ATHR73
AVAL162
AGLY165
AGLU193
APHE211
AHOH1041
AHOH1141
AHOH1208
AHOH1214
AARG8
AGLU9
ALYS60
AGLY62
AASN67
AGLY68
AGLY69
APHE70

site_idAC2
Number of Residues17
Detailsbinding site for residue N2D B 901
ChainResidue
BASP6
BARG8
BGLU9
BLYS60
BGLY62
BASN67
BGLY68
BGLY69
BPHE70
BMET71
BTHR73
BVAL162
BGLY165
BGLU193
BPHE211
BHOH1037
BHOH1093

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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