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PDBsum entry 2x1u

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
2x1u
Jmol
Contents
Protein chains
232 a.a. *
Ligands
SO4 ×6
Waters ×434
* Residue conservation analysis
PDB id:
2x1u
Name: Isomerase
Title: Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Structure: Triosephosphate isomerase, glycosomal. Chain: a, b. Fragment: residues 2-13,15-72,80-234,238-250. Synonym: tim, triose-phosphate isomerase. Engineered: yes. Mutation: yes
Source: Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.84Å     R-factor:   0.185     R-free:   0.237
Authors: M.Salin,E.G.Kapetaniou,M.Vaismaa,M.Lajunen,M.G.Casteleijn,P. L.Salmon,R.Wierenga
Key ref: M.Salin et al. (2010). Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase. Acta Crystallogr D Biol Crystallogr, 66, 934-944. PubMed id: 20693693
Date:
04-Jan-10     Release date:   26-Jan-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04789  (TPIS_TRYBB) -  Triosephosphate isomerase, glycosomal
Seq:
Struc:
250 a.a.
232 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 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!
  Cellular component     glycosome   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
Acta Crystallogr D Biol Crystallogr 66:934-944 (2010)
PubMed id: 20693693  
 
 
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase.
M.Salin, E.G.Kapetaniou, M.Vaismaa, M.Lajunen, M.G.Casteleijn, P.Neubauer, L.Salmon, R.K.Wierenga.
 
  ABSTRACT  
 
No abstract given.