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PDBsum entry 4jb1

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protein ligands links
Oxidoreductase PDB id
4jb1

 

 

 

 

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Contents
Protein chain
337 a.a.
Ligands
FAD
NAP
GOL ×6
Waters ×164
PDB id:
4jb1
Name: Oxidoreductase
Title: Crystal structure of p. Aeruginosa murb in complex with NADP+
Structure: Udp-n-acetylenolpyruvoylglucosamine reductase. Chain: a. Synonym: udp-n-acetylmuramate dehydrogenase. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Gene: murb, pa2977. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.183     R-free:   0.236
Authors: M.W.Chen,B.Lohkamp,R.Schnell,J.Lescar,G.Schneider
Key ref: M.W.Chen et al. (2013). Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates. Plos One, 8, e66936. PubMed id: 23805286 DOI: 10.1371/journal.pone.0066936
Date:
19-Feb-13     Release date:   17-Jul-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9HZM7  (MURB_PSEAE) -  UDP-N-acetylenolpyruvoylglucosamine reductase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
339 a.a.
337 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.98  - UDP-N-acetylmuramate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-N-acetyl-alpha-D-muramate + NADP+ = UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
UDP-N-acetyl-alpha-D-muramate
Bound ligand (Het Group name = NAP)
corresponds exactly
+ NADP(+)
= UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine
+ NADPH
+ H(+)
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1371/journal.pone.0066936 Plos One 8:e66936 (2013)
PubMed id: 23805286  
 
 
Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates.
M.W.Chen, B.Lohkamp, R.Schnell, J.Lescar, G.Schneider.
 
  ABSTRACT  
 
No abstract given.

 

 

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