PDBe 2qcu

X-ray diffraction
1.75Å resolution

Crystal structure of Glycerol-3-phosphate Dehydrogenase from Escherichia coli

Released:

Function and Biology Details

Reaction catalysed:
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. 
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aerobic glycerol-3-phosphate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 501 amino acids
Theoretical weight: 56.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P13035 (Residues: 1-501; Coverage: 100%)
Gene names: JW3389, b3426, glpD, glyD
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA, APS BEAMLINE 22-ID
Spacegroup: I222
Unit cell:
a: 113.791Å b: 114.097Å c: 192.801Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.24
Expression system: Escherichia coli