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3CKI

Crystal structure of the TACE-N-TIMP-3 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
B0008191molecular_functionmetalloendopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS405
AHIS409
AHIS415
BCYS1

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
AHOH689
AHOH701
AASP342
APHE343
AGLY346
AASN389
ATYR390

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF
ChainResidueDetails
AVAL402-PHE411

site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCsPsHPQdaFC
ChainResidueDetails
BCYS1-CYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18638486, ECO:0007744|PDB:3CKI
ChainResidueDetails
BCYS1

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Involved in metalloproteinase-binding => ECO:0000269|PubMed:18638486, ECO:0007744|PDB:3CKI
ChainResidueDetails
BGLU62
AHIS409
AHIS415

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN264
AGLN452

221371

PDB entries from 2024-06-19

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