2cvo

X-ray diffraction
2.2Å resolution

Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa)

Released:

Function and Biology Details

Reaction catalysed:
N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-179401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 40 KDa
Source organism: Oryza sativa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6AV34 (Residues: 50-415; Coverage: 88%)
Gene names: LOC_Os03g42110, OSJNBa0063J18.8, Os03g0617900
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P61
Unit cell:
a: 86.112Å b: 86.112Å c: 316.333Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.171 0.213
Expression system: Escherichia coli BL21(DE3)