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1EF7

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgepWGerGWLrI
ChainResidueDetails
ATYR195-ILE214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"10656802","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10745011","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
ACYS31
AASN200
AHIS180

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BCYS31
BASN200
BHIS180

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN22
ACYS31
AHIS180

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN22
BCYS31
BHIS180

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN22
AASN200
AHIS180

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN22
BASN200
BHIS180

site_idMCSA1
Number of Residues4
DetailsM-CSA 953
ChainResidueDetails
AGLN22electrostatic stabiliser
ACYS31covalent catalysis, proton shuttle (general acid/base)
AHIS180proton shuttle (general acid/base)
AASN200electrostatic stabiliser, modifies pKa

site_idMCSA2
Number of Residues4
DetailsM-CSA 953
ChainResidueDetails
BGLN22electrostatic stabiliser
BCYS31covalent catalysis, proton shuttle (general acid/base)
BHIS180proton shuttle (general acid/base)
BASN200electrostatic stabiliser, modifies pKa

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PDB entries from 2025-10-08

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