› 3oey

X-ray diffraction
2Å resolution

Crystal structure of InhA_T266E:NADH complex

Released:
DOI: 10.2210/pdb3oey/pdb
PDB entry 3oey coloured by chain, front view.
PDB entry 3oey coloured by chain, side view.
PDB entry 3oey coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis.
Molle V, Gulten G, Vilchèze C, Veyron-Churlet R, Zanella-Cléon I, Sacchettini JC, Jacobs WR, Kremer L
Mol Microbiol 78 1591-605 (2010)
PMID: 21143326

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] Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 28.58 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
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


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P6222
Unit cell:
a: 98.154Å b: 98.154Å c: 139.439Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Molecular docking and structure-based drug design strategies.
Ferreira et al. (2015)
8 more

1 mention without citation

Withdrawn
(2012)