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PDBsum entry 3pln

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protein ligands links
Oxidoreductase PDB id
3pln

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
379 a.a.
Ligands
U5P
Waters ×664
PDB id:
3pln
Name: Oxidoreductase
Title: Crystal structure of klebsiella pneumoniae udp-glucose 6-dehydrogenase complexed with udp-glucose
Structure: Udp-glucose 6-dehydrogenase. Chain: a. Engineered: yes
Source: Klebsiella pneumoniae. Organism_taxid: 484021. Strain: ntuh-k2044. Gene: kp1_3701, ugd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.50Å     R-factor:   0.164     R-free:   0.190
Authors: Y.-Y.Chen,T.-P.Ko,C.-H.Lin,W.-H.Chen,A.H.-J.Wang
Key ref: Y.Y.Chen et al. (2011). Conformational change upon product binding to Klebsiella pneumoniae UDP-glucose dehydrogenase: a possible inhibition mechanism for the key enzyme in polymyxin resistance. J Struct Biol, 175, 300-310. PubMed id: 21536136
Date:
15-Nov-10     Release date:   28-Sep-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0A0J9WZA6  (A0A0J9WZA6_KLEPN) -  UDP-glucose 6-dehydrogenase from Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044
Seq:
Struc:
388 a.a.
379 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.1.1.22  - UDP-glucose 6-dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
UDP-glucose, UDP-galactose and UDP-glucuronate Biosynthesis
      Reaction: UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 3 H+
UDP-alpha-D-glucose
+ 2 × NAD(+)
+ H2O
Bound ligand (Het Group name = U5P)
matches with 58.33% similarity
= UDP-alpha-D-glucuronate
+ 2 × NADH
+ 3 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Struct Biol 175:300-310 (2011)
PubMed id: 21536136  
 
 
Conformational change upon product binding to Klebsiella pneumoniae UDP-glucose dehydrogenase: a possible inhibition mechanism for the key enzyme in polymyxin resistance.
Y.Y.Chen, T.P.Ko, C.H.Lin, W.H.Chen, A.H.Wang.
 
  ABSTRACT  
 
No abstract given.

 

 

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