› 2buf

X-ray diffraction
2.95Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylglutamate kinase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 300 amino acids
Theoretical weight: 31.75 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HTN2 (Residues: 2-301; Coverage: 100%)
Gene names: PA5323, argB
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

4 bound ligands:
Ligand NLG 10 x NLG
Ligand ADP 10 x ADP
Ligand MG 8 x MG
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 71.86Å b: 98.78Å c: 162.9Å
α: 91.49° β: 92.03° γ: 107.56°
R-values:
R R work R free
0.249 0.249 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Surprising arginine biosynthesis: a reappraisal of the enzymology and evolution of the pathway in microorganisms.
Xu et al. (2007)
7 more

4 mentions without citation

The PII-NAGK-PipX-NtcA Regulatory Axis of Cyanobacteria: A Tale of Changing Partners, Allosteric Effectors and Non-covalent Interactions.
Forcada-Nadal et al. (2018)
3 more