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X-ray diffraction
2.75Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + glycerol = ADP + sn-glycerol 3-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-128519 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol kinase Chains: O, X
Molecule details ›
Chains: O, X
Length: 487 amino acids
Theoretical weight: 53.64 KDa
Source organism: Enterococcus casseliflavus
Expression system: Escherichia coli
UniProt:
  • Canonical: O34153 (Residues: 6-492; Coverage: 96%)
Gene name: glpK
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 68.01Å b: 107.67Å c: 201.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.242 0.268
Expression system: Escherichia coli

Quick links

Citations

9 review citations

How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
Deutscher et al. (2006)
8 more

1 mention without citation

The FGGY carbohydrate kinase family: insights into the evolution of functional specificities.
Zhang et al. (2011)