› 1o20

X-ray diffraction
2Å 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 domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-194503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-glutamyl phosphate reductase Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 48.12 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYC9 (Residues: 1-415; Coverage: 100%)
Gene names: TM_0293, proA
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C222
Unit cell:
a: 105.15Å b: 111.33Å c: 86.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.203
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Proline mechanisms of stress survival.
Liang et al. (2013)
2 more

6 mentions without citation

Pyrroline-5-carboxylate synthase and proline biosynthesis: from osmotolerance to rare metabolic disease.
Pérez-Arellano et al. (2010)
5 more