spacer
spacer

PDBsum entry 2x1r

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Isomerase PDB id
2x1r
Jmol
Contents
Protein chains
232 a.a. *
Ligands
SO4 ×3
X1R ×2
Waters ×515
* Residue conservation analysis
PDB id:
2x1r
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. Other_details: a monomeric mutant of trypanosomal triosephosphate isomerase, which has a bound 3-(propylsulphonyl)propionic acid (x1r) ligand in both
Source: Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.98Å     R-factor:   0.164     R-free:   0.226
Authors: M.Salin,E.G.Kapetaniou,M.Vaismaa,M.Lajunen,M.G.Casteleijn, P.Neubauer,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)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     glycosome   2 terms 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
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.