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2RJQ

Crystal structure of ADAMTS5 with inhibitor bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHEIGHLL
ChainResidueDetails
ATHR407-LEU416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues209
DetailsDomain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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