X-ray diffraction
3.8Å resolution

Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae


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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 95.24Å b: 111.29Å c: 113.14Å
α: 75.77° β: 89.29° γ: 69.12°
R R work R free
0.199 0.197 0.236
Expression system: Escherichia coli BL21(DE3)