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PDBsum entry 3eom

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
3eom

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
387 a.a. *
Waters ×167
* Residue conservation analysis
PDB id:
3eom
Name: Oxidoreductase
Title: 2.4 a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei
Structure: Glutaryl-coa dehydrogenase. Chain: a, b, c, d. Engineered: yes
Source: Burkholderia pseudomallei. Organism_taxid: 320372. Strain: 1710b. Gene: burps1710b_2458, burps1710b_3237, msrb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.213     R-free:   0.264
Authors: Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: D.W.Begley et al. (2011). Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1060-1069. PubMed id: 21904051
Date:
28-Sep-08     Release date:   21-Oct-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q3JP94  (Q3JP94_BURP1) -  glutaryl-CoA dehydrogenase (ETF) from Burkholderia pseudomallei (strain 1710b)
Seq:
Struc:
395 a.a.
387 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.8.6  - glutaryl-CoA dehydrogenase (ETF).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: glutaryl-CoA + oxidized [electron-transfer flavoprotein] + 2 H+ = (2E)- butenoyl-CoA + reduced [electron-transfer flavoprotein] + CO2
glutaryl-CoA
+ oxidized [electron-transfer flavoprotein]
+ 2 × H(+)
= (2E)- butenoyl-CoA
+ reduced [electron-transfer flavoprotein]
+ CO2
      Cofactor: FAD
FAD
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1060-1069 (2011)
PubMed id: 21904051  
 
 
Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening.
D.W.Begley, D.R.Davies, R.C.Hartley, S.N.Hewitt, A.L.Rychel, P.J.Myler, W.C.Van Voorhis, B.L.Staker, L.J.Stewart.
 
  ABSTRACT  
 
No abstract given.

 

 

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