› 3fne

X-ray diffraction
1.98Å resolution

Crystal structure of InhA bound to triclosan derivative 17

Released:
DOI: 10.2210/pdb3fne/pdb
PDB entry 3fne coloured by chain, front view.
PDB entry 3fne coloured by chain, side view.
PDB entry 3fne coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Triclosan derivatives: towards potent inhibitors of drug-sensitive and drug-resistant Mycobacterium tuberculosis.
Freundlich JS, Wang F, Vilchèze C, Gulten G, Langley R, Schiehser GA, Jacobus DP, Jacobs WR, Sacchettini JC
ChemMedChem 4 241-8 (2009)
PMID: 19130456

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: 28.55 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
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 4 x NAD
1 bound ligand:
Ligand 8PC 4 x 8PC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 125.593Å b: 92.34Å c: 103.016Å
α: 90° β: 106.4° γ: 90°
R-values:
R R work R free
0.203 0.201 0.253
Expression system: Escherichia coli

Quick links

Citations

22 review citations

The Halogen Bond.
Cavallo et al. (2016)
21 more

4 mentions without citation

A slow, tight binding inhibitor of InhA, the enoyl-acyl carrier protein reductase from Mycobacterium tuberculosis.
Luckner et al. (2010)
3 more