› 1tre

X-ray diffraction
2.6Å resolution

THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1tre/pdb
PDB entry 1tre coloured by chain, front view.
PDB entry 1tre coloured by chain, side view.
PDB entry 1tre coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution.
Noble ME, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont AC, Martial JA
Acta Crystallogr D Biol Crystallogr 49 403-17 (1993)
PMID: 15299515

Function and Biology Details

Reaction catalysed: 
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-141667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 27 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A858 (Residues: 1-255; Coverage: 100%)
Gene names: JW3890, b3919, tpi, tpiA
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
Spacegroup: P212121
Unit cell:
a: 67.69Å b: 46.78Å c: 151.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.119 not available
Expression system: Not provided

Quick links

Citations

35 citation in other articles

Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket.
Engel et al. (1996)
34 more

18 mentions without citation

Reductive genome evolution in Buchnera aphidicola.
van Ham et al. (2003)
17 more