spacer
spacer

PDBsum entry 1v94

Go to PDB code: 
protein Protein-protein interface(s) links
Oxidoreductase PDB id
1v94

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
429 a.a. *
Waters ×243
* Residue conservation analysis
PDB id:
1v94
Name: Oxidoreductase
Title: Crystal structure of isocitrate dehydrogenase from aeropyrum pernix
Structure: Isocitrate dehydrogenase. Chain: a, b. Engineered: yes
Source: Aeropyrum pernix. Organism_taxid: 56636. Gene: ape0689. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.28Å     R-factor:   0.215     R-free:   0.256
Authors: J.-J.Jeong,T.Sonoda,S.Fushinobu,H.Shoun,T.Wakagi
Key ref:
J.J.Jeong et al. (2004). Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix. Proteins, 55, 1087-1089. PubMed id: 15146507 DOI: 10.1002/prot.20121
Date:
20-Jan-04     Release date:   25-Jan-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9YE81  (Q9YE81_AERPE) -  isocitrate dehydrogenase (NADP(+)) from Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Seq:
Struc:
432 a.a.
429 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.1.1.42  - isocitrate dehydrogenase (NADP(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Citric acid cycle
      Reaction: D-threo-isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
D-threo-isocitrate
+ NADP(+)
= 2-oxoglutarate
+ CO2
+ NADPH
      Cofactor: Mn(2+) or Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1002/prot.20121 Proteins 55:1087-1089 (2004)
PubMed id: 15146507  
 
 
Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix.
J.J.Jeong, T.Sonoda, S.Fushinobu, H.Shoun, T.Wakagi.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Overall view of ApIDH dimer. Chains A and B are colored red and green, respectively. The three domains are indicated. The cysteine residues that form the disulfide bonds are shown as a ball-and-stick model.
Figure 2.
Figure 2. Comparison of the monomer structures of (a) ApIDH, (b) BsIDH and (c) EcIDH. Helices and strands are colored red and yellow respectively. The serine residue targeted for phophorylation of EcIDH (Ser113) and the corresponding residues of other IDHs are represented by black spheres.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 55, 1087-1089) copyright 2004.  
  Figures were selected by an automated process.  

 

spacer

spacer