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2FV9

Crystal structure of TACE in complex with JMV 390-1

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
AINN9
AHIS405
AHIS409
AHIS415

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 4
ChainResidue
B0022
BHIS405
BHIS409
BHIS415

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE INN A 9
ChainResidue
AGLU327
ASER330
ALYS331
AMET345
AGLY346
ATHR347
ALEU348
AGLY349
AASN389
ATYR390
AHIS405
AGLU406
AHIS409
AHIS415
ATYR436
APRO437
AILE438
AALA439
AHOH480
AHOH483
AZN1

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 002 B 2
ChainResidue
BZN4
BMET345
BGLY346
BTHR347
BLEU348
BGLY349
BASN389
BTYR390
BGLU398
BVAL402
BHIS405
BGLU406
BHIS409
BHIS415
BPRO437
BALA439
BVAL440
BHOH495
BHOH528

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 2024-10-09

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