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X-ray diffraction
2Å resolution

Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 --> Asp Obtained Using Microfluidic Crystallization Devices

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 526 amino acids
Theoretical weight: 59.2 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F3 (Residues: 2-501; Coverage: 100%)
Gene names: JW3897, b3926, glpK
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-3
Spacegroup: P21
Unit cell:
a: 91.116Å b: 114.26Å c: 212.624Å
α: 90° β: 91.15° γ: 90°
R-values:
R R work R free
0.168 0.167 0.225
Expression system: Escherichia coli