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PDBsum entry 2y70

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
2y70
Jmol
Contents
Protein chains
245 a.a.
Ligands
SO4 ×4
ACT ×17
Waters ×562
PDB id:
2y70
Name: Isomerase
Title: Crystallographic structure of gm23, mutant g89d, an example of catalytic migration from tim to thiamin phosphate synthase.
Structure: Triose-phosphate isomerase. Chain: a, b, c, d. Synonym: gm23, tim. Engineered: yes. Mutation: yes
Source: Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.30Å     R-factor:   0.201     R-free:   0.230
Authors: G.Saab-Rincon,L.Olvera,M.Olvera,E.Rudino-Pinera,X.Soberon,E.
Key ref: G.Saab-Rincón et al. (2012). Evolutionary walk between (β/α)(8) barrels: catalytic migration from triosephosphate isomerase to thiamin phosphate synthase. J Mol Biol, 416, 255-270. PubMed id: 22226942 DOI: 10.1016/j.jmb.2011.12.042
Date:
27-Jan-11     Release date:   07-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04789  (TPIS_TRYBB) -  Triosephosphate isomerase, glycosomal
Seq:
Struc:
250 a.a.
245 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 23 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.1  - Triose-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate
D-glyceraldehyde 3-phosphate
= glycerone phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.jmb.2011.12.042 J Mol Biol 416:255-270 (2012)
PubMed id: 22226942  
 
 
Evolutionary walk between (β/α)(8) barrels: catalytic migration from triosephosphate isomerase to thiamin phosphate synthase.
G.Saab-Rincón, L.Olvera, M.Olvera, E.Rudiño-Piñera, E.Benites, X.Soberón, E.Morett.
 
  ABSTRACT  
 
No abstract given.