X-ray diffraction
3.25Å resolution

Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae complexed with its substrate N- acetylglutamate


Function and Biology Details

Reactions catalysed:
N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetylglutamate kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 464 amino acids
Theoretical weight: 51.34 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q01217 (Residues: 58-513; Coverage: 53%)
Gene names: ARG5,6, YER069W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 92.883Å b: 103.269Å c: 111.313Å
α: 77.31° β: 89.27° γ: 70.43°
R R work R free
0.195 0.193 0.238
Expression system: Escherichia coli BL21(DE3)