› 1r2s

X-ray diffraction
2.85Å resolution

CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE

Released:
DOI: 10.2210/pdb1r2s/pdb
PDB entry 1r2s coloured by chain, front view.
PDB entry 1r2s coloured by chain, side view.
PDB entry 1r2s coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
Aparicio R, Ferreira ST, Polikarpov I
J Mol Biol 334 1023-41 (2003)
PMID: 14643664

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-133699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 248 amino acids
Theoretical weight: 26.66 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00939 (Residues: 2-249; Coverage: 100%)
Gene name: TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 73.229Å b: 80.289Å c: 174.283Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.212

Quick links

Citations

3 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
2 more

2 mentions without citation

Enantiospecificity of chloroperoxidase-catalyzed epoxidation: biased molecular dynamics study of a cis-β-methylstyrene/chloroperoxidase-compound I complex.
Morozov et al. (2011)
1 more