› 1mo0

X-ray diffraction
1.7Å resolution

Structural Genomics Of Caenorhabditis Elegans: Triose Phosphate Isomerase

Released:
DOI: 10.2210/pdb1mo0/pdb
PDB entry 1mo0 coloured by chain, front view.
PDB entry 1mo0 coloured by chain, side view.
PDB entry 1mo0 coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Structural genomics of Caenorhabditis elegans: triosephosphate isomerase.
Symersky J, Li S, Carson M, Luo M
Proteins 51 484-6 (2003)
PMID: 12696058

Function and Biology Details

Reactions catalysed: 
Glycerone phosphate = methylglyoxal + phosphate
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171243 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 29.88 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q10657 (Residues: 2-247; Coverage: 100%)
Gene names: Y17G7B.7, tpi-1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 36.399Å b: 64.373Å c: 105.706Å
α: 90° β: 91.53° γ: 90°
R-values:
R R work R free
0.183 0.183 0.213
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature.
Walden et al. (2004)
3 more

9 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
8 more