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PDBsum entry 3psw

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Isomerase PDB id
3psw
Jmol
Contents
Protein chains
246 a.a.
Ligands
EDO ×3
SO4 ×2
Waters ×475
PDB id:
3psw
Name: Isomerase
Title: Structure of e97q mutant of tim from plasmodium falciparum
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim, triose-phosphate isomerase. Engineered: yes. Mutation: yes
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: tpi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.99Å     R-factor:   0.203     R-free:   0.254
Authors: M.Samanta,M.R.N.Murthy,H.Balaram,P.Balaram
Key ref: M.Samanta et al. (2011). Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue. Chembiochem, 12, 1886-1896. PubMed id: 21671330
Date:
02-Dec-10     Release date:   19-Oct-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q07412  (TPIS_PLAFA) -  Triosephosphate isomerase
Seq:
Struc:
248 a.a.
246 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 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
Bound ligand (Het Group name = EDO)
matches with 40.00% similarity
= 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   4 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    Added reference    
 
 
Chembiochem 12:1886-1896 (2011)
PubMed id: 21671330  
 
 
Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue.
M.Samanta, M.R.Murthy, H.Balaram, P.Balaram.
 
  ABSTRACT  
 
No abstract given.