PDBe 1glf

X-ray diffraction
2.62Å resolution

CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION

Released:

Function and Biology Details

Reaction catalysed:
ATP + glycerol = ADP + sn-glycerol 3-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol kinase Chains: O, X, Y, Z
Molecule details ›
Chains: O, X, Y, Z
Length: 501 amino acids
Theoretical weight: 56.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F3 (Residues: 2-502; Coverage: 100%)
Gene names: JW3897, b3926, glpK
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 92.1Å b: 117.4Å c: 108.4Å
α: 90° β: 93.1° γ: 90°
R-values:
R R work R free
0.146 0.146 not available
Expression system: Escherichia coli