8cdf

X-ray diffraction
1.77Å resolution

Structure of glutarate hydroxylase (GlaH) from Escherichia coli at a resolution of 1.8 angstrom obtained as a contaminant during routine use of E. coli as an expression host

Released:
Source organism: Escherichia coli
Entry authors: Adeyeye AA, Schubert W

Function and Biology Details

Reaction catalysed:
Glutarate + 2-oxoglutarate + O(2) = (S)-2-hydroxyglutarate + succinate + CO(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-550627 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutarate 2-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 35.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P76621 (Residues: 15-325; Coverage: 96%)
Gene names: JW5427, b2659, csiD, gab, glaH, ygaT
Sequence domains: CsiD

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: I422
Unit cell:
a: 121.132Å b: 121.132Å c: 136.487Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.23
Expression system: Escherichia coli