3zzh

X-ray diffraction
2.1Å resolution

Crystal structure of the amino acid kinase domain from Saccharomyces cerevisiae acetylglutamate kinase in complex with its feed- back inhibitor L-arginine

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylglutamate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 307 amino acids
Theoretical weight: 34.02 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q01217 (Residues: 58-356; Coverage: 35%)
Gene names: ARG5,6, YER069W
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P212121
Unit cell:
a: 69.489Å b: 99.596Å c: 189.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.215
Expression system: Escherichia coli BL21(DE3)