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3KMC

Crystal structure of catalytic domain of TACE with tartrate-based 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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS405
AHIS409
AHIS415
AINN485
AHOH493

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE INN A 485
ChainResidue
AMET345
AGLY346
ATHR347
ALEU348
AGLY349
AASN389
ATYR390
AHIS405
AGLU406
AHIS409
AHIS415
ATYR436
APRO437
AILE438
AALA439
AHOH490
AHOH493
BARG357
AZN1
AHOH167
AGLU327
ASER330

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BHIS405
BHIS409
BHIS415
B403485

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 403 B 485
ChainResidue
BZN2
BTHR347
BLEU348
BGLY349
BLEU350
BHIS405
BGLU406
BHIS409
BHIS415
BVAL434
BTYR436
BALA439
BVAL440
BHOH553
BHOH562
BHOH566

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

237735

PDB entries from 2025-06-18

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