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3TRR

Crystal structure of a probable enoyl-CoA hydratase/isomerase from Mycobacterium abscessus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0006631biological_processfatty acid metabolic process
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0006631biological_processfatty acid metabolic process
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0006631biological_processfatty acid metabolic process
D0003824molecular_functioncatalytic activity
D0004300molecular_functionenoyl-CoA hydratase activity
D0006631biological_processfatty acid metabolic process
E0003824molecular_functioncatalytic activity
E0004300molecular_functionenoyl-CoA hydratase activity
E0006631biological_processfatty acid metabolic process
F0003824molecular_functioncatalytic activity
F0004300molecular_functionenoyl-CoA hydratase activity
F0006631biological_processfatty acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 253
ChainResidue
CGLN9
CASP11
CHOH385
CHOH449

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 253
ChainResidue
ASER231
AASP233
AALA234
CGLY130
AGLY195
APRO196
ALEU197
AALA198
AILE228

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 260
ChainResidue
AASN143
BPRO142
BASN143
BHOH258
BHOH319
CASN143

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL E 260
ChainResidue
DASN143
DHOH272
EASN143
FASN143

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG F 253
ChainResidue
ASER71
FALA74
FVAL75
FLEU76
FHOH491

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVEGfalAGGtelvLsCDL
ChainResidueDetails
AILE93-LEU113

246704

PDB entries from 2025-12-24

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