› 1vjc

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 44.49 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: Q7SIB7 (Residues: 2-417; Coverage: 100%)
Gene name: PGK1
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 36.2Å b: 106.5Å c: 51.1Å
α: 90° β: 97.6° γ: 90°
R-values:
R R work R free
0.182 0.173 0.233

Quick links

Citations

5 review citations

Nucleoside 5'-triphosphates: self-association, acid-base, and metal ion-binding properties in solution.
Sigel et al. (2005)
4 more

3 mentions without citation

Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase.
Gondeau et al. (2008)
2 more