PDBsum entry 2uvd

Go to PDB code: 
protein Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
(+ 2 more) 246 a.a. *
Waters ×575
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: The crystal structure of a 3-oxoacyl-(acyl carrier protein) reductase from bacillus anthracis (ba3989)
Structure: 3-oxoacyl-(acyl-carrier-protein) reductase. Chain: a, b, c, d, e, f, g, h. Synonym: 3-oxoacyl-acyl carrier protein reductase. Engineered: yes
Source: Bacillus anthracis. Organism_taxid: 198094. Strain: ames. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.40Å     R-factor:   0.182     R-free:   0.225
Authors: N.R.Zaccai,L.G.Carter,N.S.Berrow,S.Sainsbury,J.E.Nettleship, T.S.Walter,K.Harlos,R.J.Owens,K.S.Wilson,D.I.Stuart, R.M.Esnouf,Oxford Protein Production Facility (Oppf), Structural Proteomics In Europe (Spine)
Key ref:
N.R.Zaccai et al. (2008). Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution. Proteins, 70, 562-567. PubMed id: 17894349 DOI: 10.1002/prot.21624
09-Mar-07     Release date:   17-Apr-07    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q81JG6  (Q81JG6_BACAN) -  3-oxoacyl-(Acyl-carrier-protein) reductase
246 a.a.
246 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 3-oxoacyl-[acyl-carrier-protein] reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl- carrier-protein] + NADPH
+ NADP(+)
= 3-oxoacyl-[acyl- carrier-protein]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  


DOI no: 10.1002/prot.21624 Proteins 70:562-567 (2008)
PubMed id: 17894349  
Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution.
N.R.Zaccai, L.G.Carter, N.S.Berrow, S.Sainsbury, J.E.Nettleship, T.S.Walter, K.Harlos, R.J.Owens, K.S.Wilson, D.I.Stuart, R.M.Esnouf.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. Schematic of the reaction catalyzed by 3-oxoacyl-(ACP) reductase.
Figure 2.
Figure 2. Structure of 3-oxoacyl-(ACP) reductase. (A) The overall structure of the monomer. The model is coloured from blue at the N-terminus to red at the C-terminus and secondary structural elements are labelled. (B) Sequence alignment of B. anthracis 3-oxoacyl-(ACP) reductase (top) with its homologue from Brassica napus. Conserved residues are highlighted in red and the catalytic Ser-Tyr-Lys triad is indicated by green triangles. Residue numbering and secondary structural elements relate to the B. anthracis enzyme. (C) A model for the active site of B. anthracis 3-oxoacyl-(ACP) reductase showing the proposed binding mode for NADP+. The position of the cofactor was inferred by superposition of the B. anthracis and B. napus (PDB ID 1EDO) structures. The secondary structure of the B. anthracis enzyme is shown in grey with residues predicted to interact with NADP+ shown as black sticks. NADP+ is shown as atom-coloured sticks with yellow carbon atoms and the catalytic triad is shown as atom-coloured sticks with green carbon atoms. (D) The proposed reaction mechanism showing the role of the catalytic triad in facilitating hydride transfer from NADPH.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 70, 562-567) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21081168 D.Dutta, S.Bhattacharyya, S.Mukherjee, B.Saha, and A.K.Das (2011).
Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.
  J Struct Biol, 174, 147-155.
PDB code: 3m1l
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.