› 1gsj

X-ray diffraction
1.85Å resolution

Selenomethionine substituted N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate n-acetyl-L-glutamate and its substrate analog AMPPNP

Released:
DOI: 10.2210/pdb1gsj/pdb
PDB entry 1gsj coloured by chain, front view.
PDB entry 1gsj coloured by chain, side view.
PDB entry 1gsj coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.
Ramón-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V
Structure 10 329-42 (2002)
PMID: 12005432

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylglutamate kinase Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 27.56 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6C8 (Residues: 1-258; Coverage: 100%)
Gene names: JW5553, argB, b3959
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

3 bound ligands:
Ligand NLG 1 x NLG
Ligand ANP 1 x ANP
Ligand MG 1 x MG
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2221
Unit cell:
a: 59.564Å b: 72.332Å c: 107.418Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.227
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Genes, enzymes and regulation of arginine biosynthesis in plants.
Slocum RD. (2005)
13 more