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2OP3

The structure of cathepsin S with a novel 2-arylphenoxyacetaldehyde inhibitor derived by the Substrate Activity Screening (SAS) method

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 Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
ASER103
AHOH925
ASER103
AARG106
AARG106
AHOH734
AHOH861
AHOH861
AHOH892
AHOH892

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TF5 A 501
ChainResidue
AGLN19
AGLY23
AALA24
ACYS25
ATRP26
AASN67
AGLY68
AGLY69
AMET71
AGLY137
AASN163
AHIS164
AGLY165
APEU601
AHOH912

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TF5 B 502
ChainResidue
APEU601
BGLN19
BGLY23
BALA24
BCYS25
BTRP26
BASN67
BGLY68
BGLY69
BMET71
BGLY137
BASN163
BHIS164
BGLY165

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEU A 601
ChainResidue
APHE70
ATF5501
AHOH891
AHOH940
BGLY69
BPHE70
BTF5502

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGACWAfSA
ChainResidueDetails
AGLN19-ALA30

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
ACYS25
AHIS164
AASN184
BCYS25
BHIS164
BASN184

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
ACYS25
AASN184

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS164
BCYS25
BASN184

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
ACYS25

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS164
BGLN19
BCYS25

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
AASN184

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS164
BGLN19
BASN184

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
ACYS25
AASN184

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS164
BGLN19
BCYS25
BASN184

site_idMCSA1
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
AGLN19electrostatic stabiliser
ACYS25nucleofuge, nucleophile, proton acceptor, proton donor
AHIS164proton acceptor, proton donor
AASN184electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
BGLN19electrostatic stabiliser
BCYS25nucleofuge, nucleophile, proton acceptor, proton donor
BHIS164proton acceptor, proton donor
BASN184electrostatic stabiliser

219140

PDB entries from 2024-05-01

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