X-ray diffraction
2.25Å resolution

Function and Biology Details

Reaction catalysed:
L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Gamma-glutamyl phosphate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 444 amino acids
Theoretical weight: 47.66 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli
  • Canonical: Q2SZ88 (Residues: 1-423; Coverage: 100%)
Gene names: BTH_I1214, proA
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 85.41Å b: 142.46Å c: 154.76Å
α: 90° β: 90° γ: 90°
R R work R free
0.183 0.18 0.224
Expression system: Escherichia coli