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PDBsum entry 3a12

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3a12
Jmol
Contents
Protein chains
(+ 4 more) 437 a.a. *
Ligands
CAP ×10
Metals
_MG ×10
Waters ×2306
* Residue conservation analysis
PDB id:
3a12
Name: Lyase
Title: Crystal structure of type iii rubisco complexed with 2-cabp
Structure: Ribulose bisphosphate carboxylase. Chain: a, b, c, d, e, f, g, h, i, j. Synonym: rubisco. Engineered: yes
Source: Pyrococcus kodakaraensis. Thermococcus kodakaraensis. Organism_taxid: 69014. Strain: kod1. Gene: rbcl, tk2290. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.30Å     R-factor:   0.201     R-free:   0.244
Authors: Y.Nishitani,M.Fujihashi,T.Doi,S.Yoshida,H.Atomi,T.Imanaka,K.
Key ref: Y.Nishitani et al. (2010). Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile. J Biol Chem, 285, 39339-39347. PubMed id: 20926376
Date:
25-Mar-09     Release date:   07-Apr-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O93627  (RBL_PYRKO) -  Ribulose bisphosphate carboxylase
Seq:
Struc:
444 a.a.
437 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.39  - Ribulose-bisphosphate carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
2 × 3-phospho-D-glycerate
+ 2 × H(+)
=
D-ribulose 1,5-bisphosphate
Bound ligand (Het Group name = CAP)
matches with 85.71% similarity
+ CO(2)
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
J Biol Chem 285:39339-39347 (2010)
PubMed id: 20926376  
 
 
Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile.
Y.Nishitani, S.Yoshida, M.Fujihashi, K.Kitagawa, T.Doi, H.Atomi, T.Imanaka, K.Miki.
 
  ABSTRACT  
 
No abstract given.