› 1bvr

X-ray diffraction
2.8Å resolution

M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE

Released:
DOI: 10.2210/pdb1bvr/pdb
PDB entry 1bvr coloured by chain, front view.
PDB entry 1bvr coloured by chain, side view.
PDB entry 1bvr coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.
Rozwarski DA, Vilchèze C, Sugantino M, Bittman R, Sacchettini JC
J Biol Chem 274 15582-9 (1999)
PMID: 10336454

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 domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161511 (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: 268 amino acids
Theoretical weight: 28.42 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WGR1 (Residues: 2-269; 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 6 x NAD
1 bound ligand:
Ligand THT 4 x THT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 101.08Å b: 83.45Å c: 192.81Å
α: 90° β: 95.24° γ: 90°
R-values:
R R work R free
0.217 0.217 0.344
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh et al. (2008)
16 more

26 mentions without citation

Targeting InhA, the FASII enoyl-ACP reductase: SAR studies on novel inhibitor scaffolds.
Pan et al. (2012)
25 more