› 1eny

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS

Released:
DOI: 10.2210/pdb1eny/pdb
PDB entry 1eny coloured by chain, front view.
PDB entry 1eny coloured by chain, side view.
PDB entry 1eny coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
Dessen A, Quémard A, Blanchard JS, Jacobs WR, Sacchettini JC
Science 267 1638-41 (1995)
PMID: 7886450

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 dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-161511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 28.39 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 1 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6222
Unit cell:
a: 100.14Å b: 100.14Å c: 140.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 not available
Expression system: Escherichia coli

Quick links

Citations

52 review citations

Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis.
Takayama et al. (2005)
51 more

24 mentions without citation

A Structure-Based Drug Discovery Paradigm.
Batool et al. (2019)
23 more