1ENZ Oxidoreductase date Jan 27, 1995
authors A.Dessen, A.Quemard, J.S.Blanchard, W.R.Jacobs Jr., J.C.Sacchettini, Tb Structural Genomics Consortium (Tbsgc)
compound source
Molecule: Enoyl-Acyl Carrier Protein (Acp) Reductase
Chain: Null
Synonym: Inha
Engineered: Yes
Mutation: S94a
Organism_scientific: Mycobacterium Tuberculosis
Expression_system: Escherichia Coli
symmetry Space Group: P 62 2 2
R_factor 0.193
crystal
cell
length a length b length c angle alpha angle beta angle gamma
100.140 100.140 139.950 90.00 90.00 120.00
method X-Ray Diffractionresolution 2.7 Å
ligand NAD enzyme
similarity Fabisubfamily. Belongs to the short-chain dehydrogenases/reductases (sdr) family.
subunit Homotetramer.
catalytic activ. Acyl-[acyl-carrier protein] + nad(+) = trans- 2,3-dehydroacyl-[acyl-carrier protein] + nadh.
pathway Second reductive step in fatty acid biosynthesis. This isozyme is involved in mycolic acid biosynthesis.
genes MT1531, inhA (M. tuberculosis)
function Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide.
Gene
Ontology
ChainFunctionProcessComponent
A
  • enoyl-[acyl-carrier-protein]...
  • oxidoreductase activity
  • fatty acid biosynthetic proc...
  • metabolic process
  • lipid biosynthetic process
  • response to antibiotic

  • Primary referenceCrystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science 1995 Mar 17;267(5204):1638-41. PMID:7886450
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (53 Kb) [Save to disk]
  • Biological Unit Coordinates (1enz.pdb1.gz) 82 Kb
  • CSU: Contacts of Structural Units for 1ENZ
  • Likely Quarternary Molecular Structure file(s) for 1ENZ
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