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1ZXC

Crystal structure of catalytic domain of TNF-alpha converting enzyme (TACE) with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS405
AHIS409
AHIS415
AIH6478

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 202
ChainResidue
BHIS405
BHIS409
BHIS415
BIH6478

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE IH6 A 478
ChainResidue
AHOH56
AZN201
ATHR347
ALEU348
AGLY349
ALEU350
ALEU401
AVAL402
AHIS405
AGLU406
AHIS409
AHIS415
AVAL434
APRO437
AVAL440
AHOH16

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE IH6 B 478
ChainResidue
BHOH110
BZN202
BGLU290
BGLY346
BTHR347
BLEU348
BGLY349
BGLU398
BLEU401
BHIS405
BGLU406
BHIS409
BHIS415
BVAL434
BALA439
BVAL440

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9520379
ChainResidueDetails
AGLU406
BGLU406

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9520379
ChainResidueDetails
AHIS405
AHIS409
AHIS415
BHIS405
BHIS409
BHIS415

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN264
AGLN452
BASN264
BGLN452

223790

PDB entries from 2024-08-14

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