› 4iot

X-ray diffraction
1.85Å resolution

High-resolution Structure of Triosephosphate isomerase from E. coli

Released:
DOI: 10.2210/pdb4iot/pdb
PDB entry 4iot coloured by chain, front view.
PDB entry 4iot coloured by chain, side view.
PDB entry 4iot coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. DH10B
Primary publication:
Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli.
Kozlov G, Vinaik R, Gehring K
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 499-502 (2013)
PMID: 23695562

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109424 (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 str. K-12 substr. DH10B
UniProt:
  • Canonical: B1XB85 (Residues: 1-255; Coverage: 100%)
Gene names: ECDH10B_4108, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 46.47Å b: 67.452Å c: 150.354Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.206

Quick links

Citations

5 citation in other articles

ContaMiner and ContaBase: a webserver and database for early identification of unwantedly crystallized protein contaminants.
Hungler et al. (2016)
4 more

3 mentions without citation

Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli.
Kozlov et al. (2013)
2 more