Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2I47

Crystal structure of catalytic domain of 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
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
D0004222molecular_functionmetalloendopeptidase activity
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 801
ChainResidue
BHIS405
BHIS409
BHIS415
BINN902

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 802
ChainResidue
AHIS405
AHIS409
AHIS415
AINN901

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 803
ChainResidue
DHIS409
DHIS415
DKGY1002
DHIS405

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 804
ChainResidue
CHIS405
CHIS409
CHIS415
CKGY1001

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE INN A 901
ChainResidue
AMET345
AGLY346
ATHR347
ALEU348
AGLY349
AASN389
ATYR390
AHIS405
AGLU406
AHIS409
AHIS415
APRO437
AILE438
AALA439
AZN802
AHOH927
AHOH958
AHOH987
AHOH1098

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE INN B 902
ChainResidue
BMET345
BGLY346
BTHR347
BLEU348
BGLY349
BASN389
BTYR390
BHIS405
BGLU406
BHIS409
BHIS415
BPRO437
BILE438
BALA439
BZN801
BHOH923
BHOH926

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE KGY C 1001
ChainResidue
CVAL314
CGLY346
CTHR347
CLEU348
CGLY349
CLEU350
CGLU398
CLEU401
CVAL402
CHIS405
CGLU406
CHIS409
CHIS415
CPRO437
CALA439
CVAL440
CZN804
CHOH1008
CHOH1025
CHOH1144

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE KGY D 1002
ChainResidue
DVAL314
DTHR347
DLEU348
DGLY349
DLEU350
DGLU398
DLEU401
DVAL402
DHIS405
DGLU406
DHIS409
DHIS415
DPRO437
DALA439
DVAL440
DZN803
DHOH1012
DHOH1049

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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:9520379
ChainResidueDetails
AGLU406
BGLU406
CGLU406
DGLU406

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:9520379
ChainResidueDetails
AHIS405
DHIS405
DHIS409
DHIS415
AHIS409
AHIS415
BHIS405
BHIS409
BHIS415
CHIS405
CHIS409
CHIS415

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN264
AGLN452
BASN264
BGLN452
CASN264
CGLN452
DASN264
DGLN452

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon