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3L0V

Crystal structure of catalytic domain of TACE with the first hydantoin inhibitor occupying the S1' pocket

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 1
ChainResidue
AHIS405
AHIS409
AHIS415
A724485

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 724 A 485
ChainResidue
AVAL402
AHIS405
AGLU406
AHIS409
AHIS415
ATYR436
APRO437
AALA439
AHOH495
AZN1
ATHR347
ALEU348
AGLY349
ALEU401

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BHIS405
BHIS409
BHIS415
B724485

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 724 B 485
ChainResidue
BZN2
BTHR347
BLEU348
BGLY349
BLEU401
BVAL402
BHIS405
BGLU406
BHIS409
BHIS415
BTYR436
BPRO437
BALA439
BHOH548

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

221051

PDB entries from 2024-06-12

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