PDBsum entry 2idz

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Oxidoreductase PDB id
Protein chain
268 a.a. *
Waters ×237
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of wild type enoyl-acp(coa) reductase from mycobacterium tuberculosis in complex with nadh-inh
Structure: Enoyl-[acyl-carrier-protein] reductase [nadh]. Chain: a. Synonym: nadh- dependent enoyl-acp reductase. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: inha. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
2.00Å     R-factor:   0.190     R-free:   0.226
Authors: M.V.B.Dias,M.P.X.Prado,I.B.Vasconcelos,F.Valmir,L.A.Basso,D. W.F.Azevedo Jr.
Key ref: M.V.Dias et al. (2007). Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis. J Struct Biol, 159, 369-380. PubMed id: 17588773
15-Sep-06     Release date:   24-Jul-07    
Go to PROCHECK summary

Protein chain
Protein chain
P9WGR0  (INHA_MYCTO) -  Enoyl-[acyl-carrier-protein] reductase [NADH]
269 a.a.
268 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Enoyl-[acyl-carrier-protein] reductase (NADH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH
acyl-[acyl-carrier protein]
Bound ligand (Het Group name = ZID)
matches with 84.00% similarity
= trans-2,3-dehydroacyl-[acyl- carrier protein]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell wall   2 terms 
  Biological process     mycolic acid biosynthetic process   7 terms 
  Biochemical function     oxidoreductase activity     4 terms  


J Struct Biol 159:369-380 (2007)
PubMed id: 17588773  
Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis.
M.V.Dias, I.B.Vasconcelos, A.M.Prado, V.Fadel, L.A.Basso, Azevedo, D.S.Santos.
The resumption of tuberculosis led to an increased need to understand the molecular mechanisms of drug action and drug resistance, which should provide significant insight into the development of newer compounds. Isoniazid (INH), the most prescribed drug to treat TB, inhibits an NADH-dependent enoyl-acyl carrier protein reductase (InhA) that provides precursors of mycolic acids, which are components of the mycobacterial cell wall. InhA is the major target of the mode of action of isoniazid. INH is a pro-drug that needs activation to form the inhibitory INH-NAD adduct. Missense mutations in the inhA structural gene have been identified in clinical isolates of Mycobacterium tuberculosis resistant to INH. To understand the mechanism of resistance to INH, we have solved the structure of two InhA mutants (I21V and S94A), identified in INH-resistant clinical isolates, and compare them to INH-sensitive WT InhA structure in complex with the INH-NAD adduct. We also solved the structure of unliganded INH-resistant S94A protein, which is the first report on apo form of InhA. The salient features of these structures are discussed and should provide structural information to improve our understanding of the mechanism of action of, and resistance to, INH in M. tuberculosis. The unliganded structure of InhA allows identification of conformational changes upon ligand binding and should help structure-based drug design of more potent antimycobacterial agents.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21280175 K.Maity, T.Banerjee, N.Prabakaran, N.Surolia, A.Surolia, and K.Suguna (2011).
Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from plasmodium falciparum.
  IUBMB Life, 63, 30-41.
PDB codes: 3am3 3am4 3am5
19043750 G.B.Barcellos, R.A.Caceres, and Azevedo (2009).
Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.
  J Mol Model, 15, 147-155.  
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