› 4trm

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 269 amino acids
Theoretical weight: 28.55 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P9WGR1 (Residues: 1-269; Coverage: 100%)
Gene names: MTCY277.05, Rv1484, inhA
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 100.096Å b: 81.787Å c: 187.242Å
α: 90° β: 95.62° γ: 90°
R-values:
R R work R free
0.19 0.189 0.219
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Update of Antitubercular Prodrugs from a Molecular Perspective: Mechanisms of Action, Bioactivation Pathways, and Associated Resistance.
Laborde et al. (2017)
11 other articles

4 mentions without citation

Bacterial Enoyl-Reductases: The Ever-Growing List of Fabs, Their Mechanisms and Inhibition.
Hopf et al. (2022)
3 more