› 4ghk

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.183 0.18 0.224
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

2 mentions without citation

Beyond antibody engineering: directed evolution of alternative binding scaffolds and enzymes using yeast surface display.
Könning et al. (2018)
1 more