› 1r2r

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE

Released:
DOI: 10.2210/pdb1r2r/pdb
PDB entry 1r2r coloured by chain, front view.
PDB entry 1r2r coloured by chain, side view.
PDB entry 1r2r 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

3 bound ligands:
Ligand DMS 17 x DMS
Ligand MG 9 x MG
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 74.55Å b: 75.952Å c: 166.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.19

Quick links

Citations

3 review citations

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

14 mentions without citation

Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.
Chan et al. (2005)
13 more