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Isomerase PDB id
Protein chains
257 a.a. *
ACT ×2
SO4 ×5
Waters ×461
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Structural genomics of caenorhabditis elegans: triose phosphate isomerase
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim. Engineered: yes
Source: Caenorhabditis elegans. Organism_taxid: 6239. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
1.70Å     R-factor:   0.183     R-free:   0.213
Authors: J.Symersky,S.Li,J.Finley,Z.-J.Liu,H.Qui,C.H.Luan,M.Carson, J.Tsao,D.Johnson,G.Lin,J.Zhao,W.Thomas,L.A.Nagy,B.Sha, L.J.Delucas,B.-C.Wang,M.Luo,Southeast Collaboratory For Structural Genomics (Secsg)
Key ref:
J.Symersky et al. (2003). Structural genomics of Caenorhabditis elegans: triosephosphate isomerase. Proteins, 51, 484-486. PubMed id: 12696058 DOI: 10.1002/prot.10364
06-Sep-02     Release date:   13-Sep-02    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q10657  (TPIS_CAEEL) -  Triosephosphate isomerase
247 a.a.
257 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - 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     intracellular   2 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     catalytic activity     3 terms  


    Added reference    
DOI no: 10.1002/prot.10364 Proteins 51:484-486 (2003)
PubMed id: 12696058  
Structural genomics of Caenorhabditis elegans: triosephosphate isomerase.
J.Symersky, S.Li, M.Carson, M.Luo.

  Selected figure(s)  
Figure 1.
Figure 1. Active site of C. elegans TIM with acetate and sulfate. Three structurally conserved water molecules are included as red spheres. The C. elegans structure is shown as thick atoms and bonds colored by atom type, with key residues labeled. Dashed lines represent hydrogen bonds. Comparison structures are shown in white, with smaller bonds and atomic radii. Top: Comparison to the open conformation; the 1YPI unliganded structure of chicken TIM. Bottom: Comparison to the closed conformation; the 1TPH structure of chicken TIM with phosphoglycolohydroxamate.
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2003, 51, 484-486) copyright 2003.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19261703 S.S.Thakur, P.D.Deepalakshmi, P.Gayathri, M.Banerjee, M.R.Murthy, and P.Balaram (2009).
Detection of the protein dimers, multiple monomeric states and hydrated forms of Plasmodium falciparum triosephosphate isomerase in the gas phase.
  Protein Eng Des Sel, 22, 289-304.  
17957775 C.H.Chu, Y.J.Lai, H.Huang, and Y.J.Sun (2008).
Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori.
  Proteins, 71, 396-406.
PDB code: 2jgq
  18629029 , (2003).
Current awareness on comparative and functional genomics.
  Comp Funct Genomics, 4, 681-688.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.