› 5oiq

X-ray diffraction
2.65Å 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
Molecule details ›
Chains: A, B, C, D
Length: 269 amino acids
Theoretical weight: 28.52 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WGR1 (Residues: 1-1, 3-269; 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


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand 9WB 4 x 9WB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 64.97Å b: 115.04Å c: 69.05Å
α: 90° β: 97.44° γ: 90°
R-values:
R R work R free
0.163 0.16 0.227
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Mycobacterial drug discovery.
Abrahams et al. (2020)
2 more

1 mention without citation

Screening of a Novel Fragment Library with Functional Complexity against Mycobacterium tuberculosis InhA.
Prati et al. (2018)