› 1b9b

X-ray diffraction
2.85Å resolution

Function and Biology Details

Reactions catalysed: 
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional PGK/TIM Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 28.55 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: P36204 (Residues: 400-654; Coverage: 39%)
Gene names: TM_0689, pgk/tpi
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P3221
Unit cell:
a: 125.95Å b: 125.95Å c: 103.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.211 0.249
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
6 more

10 mentions without citation

Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling: A CASP-CAPRI experiment.
Lensink et al. (2016)
9 more