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PDBsum entry 3mvo

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3mvo
Jmol
Contents
Protein chains
(+ 0 more) 495 a.a.
Ligands
GLU ×6
NDP ×6
Metals
EU3 ×2
PDB id:
3mvo
Name: Oxidoreductase
Title: Crystal structure of bovine glutamate dehydrogenase complexe eu3+
Structure: Glutamate dehydrogenase 1, mitochondrial. Chain: a, b, c, d, e, f. Fragment: glutamate dehydrogenase, residues 58-558. Synonym: gdh 1. Ec: 1.4.1.3
Source: Bos taurus. Bovine. Organism_taxid: 9913. Other_details: liver
Resolution:
3.23Å     R-factor:   0.263     R-free:   0.310
Authors: T.J.Smith,M.Li
Key ref: J.Bailey et al. (2011). A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis. FEBS J, 278, 3140-3151. PubMed id: 21749647
Date:
04-May-10     Release date:   04-May-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00366  (DHE3_BOVIN) -  Glutamate dehydrogenase 1, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
558 a.a.
495 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.4.1.3  - Glutamate dehydrogenase (NAD(P)(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-glutamate + H2O + NAD(P)(+) = 2-oxoglutarate + NH3 + NAD(P)H
L-glutamate
Bound ligand (Het Group name = GLU)
corresponds exactly
+ H(2)O
+
NAD(P)(+)
Bound ligand (Het Group name = NDP)
corresponds exactly
= 2-oxoglutarate
+ NH(3)
+ NAD(P)H
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   3 terms 
  Biological process     tricarboxylic acid metabolic process   6 terms 
  Biochemical function     nucleotide binding     7 terms  

 

 
    reference    
 
 
FEBS J 278:3140-3151 (2011)
PubMed id: 21749647  
 
 
A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis.
J.Bailey, L.Powell, L.Sinanan, J.Neal, M.Li, T.Smith, E.Bell.
 
  ABSTRACT  
 
No abstract given.