› 2ied

X-ray diffraction
2.14Å resolution

CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDUCTASE MUTANT ENZYME FROM MYCOBACTERIUM TUBERCULOSIS UNCOMPLEXED

Released:
DOI: 10.2210/pdb2ied/pdb
PDB entry 2ied coloured by chain, front view.
PDB entry 2ied coloured by chain, side view.
PDB entry 2ied 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] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P1
Unit cell:
a: 54.694Å b: 63.517Å c: 65.181Å
α: 97.21° β: 85.81° γ: 102.87°
R-values:
R R work R free
0.166 0.162 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

2 mentions without citation

Molecular docking screens using comparative models of proteins.
Fan et al. (2009)
1 more