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PDBsum entry 2wsr

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protein ligands links
Isomerase PDB id
2wsr
Jmol
Contents
Protein chain
242 a.a. *
Ligands
SO4 ×4
AZI ×2
Waters ×303
* Residue conservation analysis
PDB id:
2wsr
Name: Isomerase
Title: Monotim mutant rmm0-1, monomeric form.
Structure: Triose phosphate isomerase, glycosomal. Chain: a. Fragment: residues 2-67,84-250. Synonym: tim, triose-phosphate isomerase, monotim mutant rmm0-1. Engineered: yes. Mutation: yes
Source: Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.65Å     R-factor:   0.215     R-free:   0.255
Authors: E.Rudino-Pinera,S.P.Rojas-Trejo,R.Arreola,G.Saab-Rincon, X.Soberon,E.Horjales
Key ref: E.Rudino-Pinera et al. Space group transition driven by temperature and related to monomer-Dimer transition in solution: the case of monomeric tim of trypanosoma brucei brucei. To be published, .
Date:
08-Sep-09     Release date:   15-Sep-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04789  (TPIS_TRYBB) -  Triosephosphate isomerase, glycosomal
Seq:
Struc:
250 a.a.
242 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 10 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