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PDBsum entry 3mjs

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3mjs
Jmol
Contents
Protein chains
476 a.a. *
Ligands
NDP ×2
LMR
MLT ×3
GOL ×2
Waters ×504
* Residue conservation analysis
PDB id:
3mjs
Name: Oxidoreductase
Title: Structure of a-type ketoreductases from modular polyketide s
Structure: Amphb. Chain: a, b. Fragment: ketoreductase domain. Engineered: yes
Source: Streptomyces nodosus. Organism_taxid: 40318. Gene: amphb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.40Å     R-factor:   0.200     R-free:   0.226
Authors: J.Zheng,C.A.Taylor,S.K.Piasecki,A.T.Keatinge-Clay
Key ref: J.Zheng et al. (2010). Structural and functional analysis of A-type ketoreductases from the amphotericin modular polyketide synthase. Structure, 18, 913-922. PubMed id: 20696392
Date:
13-Apr-10     Release date:   18-Aug-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q93NW7  (Q93NW7_9ACTO) -  AmphB
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
3190 a.a.
476 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Structure 18:913-922 (2010)
PubMed id: 20696392  
 
 
Structural and functional analysis of A-type ketoreductases from the amphotericin modular polyketide synthase.
J.Zheng, C.A.Taylor, S.K.Piasecki, A.T.Keatinge-Clay.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21340070 D.H.Kwan, M.Tosin, N.Schläger, F.Schulz, and P.F.Leadlay (2011).
Insights into the stereospecificity of ketoreduction in a modular polyketide synthase.
  Org Biomol Chem, 9, 2053-2056.  
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.