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

3H81

Crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0005886cellular_componentplasma membrane
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0009274cellular_componentpeptidoglycan-based cell wall
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0005886cellular_componentplasma membrane
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0009274cellular_componentpeptidoglycan-based cell wall
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0005886cellular_componentplasma membrane
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0009274cellular_componentpeptidoglycan-based cell wall
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AALA86
AMET91
APHE105
AGLU132
ALEU158
AGLY160
AMET161
AHOH327
AHOH351

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 279
ChainResidue
APHE255
AGLN260
AHOH306
AHOH311
CLEU94
CHOH325

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 401
ChainResidue
BALA86
BGLU132
BGLU152
BLEU158
BPRO159
BGLY160
BMET161
BHOH343
BHOH362
CPHE251

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL C 401
ChainResidue
APHE251
CALA86
CPHE105
CGLU132
CGLU152
CLEU158
CPRO159
CGLY160
CMET161
CHOH304
CHOH359

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 402
ChainResidue
CPHE105
CTRP108
CALA112
CMET136
CMET161
CARG166
CHOH300
CHOH380
CHOH561

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 279
ChainResidue
AARG193
AHOH377
BARG193
BHOH307
CARG193
CHOH355

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 280
ChainResidue
BLEU94
BHOH315
BHOH337
CPHE255
CGLN260
CHOH353

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVAGyalGGGcelaMmCDV
ChainResidueDetails
AILE119-VAL139

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
AGLU152
AALA86
AGLY129
AGLU132

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
BGLU152
BALA86
BGLY129
BGLU132

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
CGLU152
CALA86
CGLY129
CGLU132

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
AGLU152
AGLY160

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
BGLU152
BGLY160

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
CGLU152
CGLY160

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
AGLU152
AGLY129
AGLU132

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
BGLU152
BGLY129
BGLU132

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dub
ChainResidueDetails
CGLU152
CGLY129
CGLU132

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon