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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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:18042673
ChainResidueDetails
AGLU411

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18042673
ChainResidueDetails
AHIS410
AHIS414
AHIS420

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18042673
ChainResidueDetails
AASN498

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: C-linked (Man) tryptophan => ECO:0000269|PubMed:19671700
ChainResidueDetails
ATRP570
ATRP573

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:19671700
ChainResidueDetails
ASER582

218853

PDB entries from 2024-04-24

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