› 1aw2

X-ray diffraction
2.65Å resolution

TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS

Released:
DOI: 10.2210/pdb1aw2/pdb
PDB entry 1aw2 coloured by chain, front view.
PDB entry 1aw2 coloured by chain, side view.
PDB entry 1aw2 coloured by chain, top view.
Source organism: Moritella marina
Primary publication:
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D
J Biol Chem 273 2199-206 (1998)
PMID: 9442062

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-156273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, D, E, G, H, J, K
Molecule details ›
Chains: A, B, D, E, G, H, J, K
Length: 256 amino acids
Theoretical weight: 26.77 KDa
Source organism: Moritella marina
Expression system: Escherichia coli
UniProt:
  • Canonical: P50921 (Residues: 1-256; Coverage: 100%)
Gene names: tim, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 89.66Å b: 137.82Å c: 89.54Å
α: 90° β: 90.94° γ: 90°
R-values:
R R work R free
0.2 0.2 0.219
Expression system: Escherichia coli

Quick links

Citations

9 review citations

The stability of proteins in extreme environments.
Jaenicke et al. (1998)
8 more

3 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
2 more