› 1vpe

X-ray diffraction
2Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF PHOSPHOGLYCERATE KINASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1vpe/pdb
PDB entry 1vpe coloured by chain, front view.
PDB entry 1vpe coloured by chain, side view.
PDB entry 1vpe coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.
Auerbach G, Huber R, Grättinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U
Structure 5 1475-83 (1997)
PMID: 9384563

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153149 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional PGK/TIM Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 43.05 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: P36204 (Residues: 2-398; Coverage: 61%)
Gene names: TM_0689, pgk/tpi
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand ANP 1 x ANP
Ligand 3PG 1 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 62.009Å b: 76.864Å c: 87.501Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.288
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

11 mentions without citation

Enhanced Diffusion of Catalytically Active Enzymes.
Zhang et al. (2019)
10 more