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PDBsum entry 3of2

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protein ligands links
Oxidoreductase PDB id
3of2
Jmol
Contents
Protein chain
267 a.a. *
Ligands
NAD
MPD
Waters ×197
* Residue conservation analysis
PDB id:
3of2
Name: Oxidoreductase
Title: Crystal structure of inha_t266d:nadh complex
Structure: Enoyl-[acyl-carrier-protein] reductase [nadh]. Chain: a. Synonym: nadh-dependent enoyl-acp reductase. Engineered: yes. Mutation: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: inha, mt1531, mtcy277.05, rv1484. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.177     R-free:   0.203
Authors: V.Molle,G.Gulten,C.Vilcheze,R.Veyron-Churlet,I.Zanella-Cleon J.C.Sacchettini,W.R.Jacobs Jr,L Kremer
Key ref: V.Molle et al. (2010). Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis. Mol Microbiol, 78, 1591-1605. PubMed id: 21143326
Date:
13-Aug-10     Release date:   01-Dec-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam  
P9WGR1  (INHA_MYCTU) -  Enoyl-[acyl-carrier-protein] reductase [NADH]
Seq:
Struc:
269 a.a.
267 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.9  - 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]
+
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
= trans-2,3-dehydroacyl-[acyl- carrier protein]
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   5 terms 
  Biochemical function     oxidoreductase activity     2 terms  

 

 
    reference    
 
 
Mol Microbiol 78:1591-1605 (2010)
PubMed id: 21143326  
 
 
Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis.
V.Molle, G.Gulten, C.Vilchèze, R.Veyron-Churlet, I.Zanella-Cléon, J.C.Sacchettini, W.R.Jacobs, L.Kremer.
 
  ABSTRACT  
 
No abstract given.