› 2ieb

X-ray diffraction
2.2Å resolution

Crystal Structure of Isoniazid-resistant S94A ENOYL-ACP(COA) Reductase Mutant Enzyme from MYCOBACTERIUM TUBERCULOSIS in Complex with NADH-INH

Released:
DOI: 10.2210/pdb2ieb/pdb
PDB entry 2ieb coloured by chain, front view.
PDB entry 2ieb coloured by chain, side view.
PDB entry 2ieb coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis.
Dias MV, Vasconcelos IB, Prado AM, Fadel V, Basso LA, de Azevedo WF, Santos DS
J Struct Biol 159 369-80 (2007)
PMID: 17588773

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

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: 268 amino acids
Theoretical weight: 28.41 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
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 ZID 1 x ZID
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P6222
Unit cell:
a: 96.83Å b: 96.83Å c: 136.418Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.24
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Antimicrobial susceptibility testing, drug resistance mechanisms, and therapy of infections with nontuberculous mycobacteria.
Brown-Elliott et al. (2012)
2 more