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3E8R

Crystal structure of catalytic domain of TACE with hydroxamate 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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AINN4
AHIS405
AHIS409
AHIS415
A615486
AHOH631

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 615 A 486
ChainResidue
ALEU348
AGLY349
AGLU398
ALEU401
AHIS405
AGLU406
AHIS409
AHIS415
ATYR433
AVAL434
ATYR436
APRO437
AALA439
AASN447
AHOH509
AHOH557
AHOH634
AHOH649
AHOH696
AZN1
AGLY346
ATHR347

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE INN A 4
ChainResidue
AZN1
AGLU327
ASER330
ALYS331
AMET345
AGLY346
ATHR347
ALEU348
AGLY349
ATYR390
AHIS405
AGLU406
AHIS409
AHIS415
ATYR436
APRO437
AILE438
AALA439
AHOH509
AHOH631
AHOH632
AHOH634
AHOH694
BARG357

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BHIS405
BHIS409
BHIS415
B615486
BHOH692

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 615 B 486
ChainResidue
BZN2
BGLY346
BTHR347
BLEU348
BGLY349
BGLU398
BLEU401
BHIS405
BGLU406
BHIS409
BHIS415
BTYR433
BVAL434
BTYR436
BPRO437
BILE438
BALA439
BVAL440
BGLY442
BASN447
BHOH652
BHOH654
BHOH692

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT B 3
ChainResidue
APRO356
AHIS415
APRO437
BARG357
BASN359
BSER360
BHIS361
BHOH556
BHOH565
BHOH732

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

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PDB entries from 2024-07-10

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