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5DU6

Crystal structure of M. tuberculosis EchA6 bound to ligand GSK059A.

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 Residues7
Detailsbinding site for residue G59 A 301
ChainResidue
ALEU75
AGLN107
AASP131
ATRP133
AALA208
ALYS213
APHE216

site_idAC2
Number of Residues8
Detailsbinding site for residue G59 B 301
ChainResidue
BGLN103
BASP131
BTRP133
BALA208
BLYS213
BPHE216
BHIS79
BASP83

site_idAC3
Number of Residues9
Detailsbinding site for residue G59 C 301
ChainResidue
CLEU75
CHIS79
CASP83
CGLN107
CASP131
CTRP133
CALA208
CLYS213
CPHE216

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VGaINGpaiGAGlqlaMqCDL
ChainResidueDetails
AVAL90-LEU110

219140

PDB entries from 2024-05-01

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