› 2j5v

X-ray diffraction
2.5Å resolution

GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-5-PHOSPHATE AND PYROGLUTAMIC ACID

Released:
DOI: 10.2210/pdb2j5v/pdb
PDB entry 2j5v coloured by chain, front view.
PDB entry 2j5v coloured by chain, side view.
PDB entry 2j5v coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase.
Marco-Marín C, Gil-Ortiz F, Pérez-Arellano I, Cervera J, Fita I, Rubio V
J Mol Biol 367 1431-46 (2007)
PMID: 17321544

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141574 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate 5-kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 39.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A7B5 (Residues: 1-367; Coverage: 100%)
Gene names: JW0232, b0242, proB
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 1 x MG
Ligand PCA 2 x PCA
Ligand RGP 2 x RGP
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P41212
Unit cell:
a: 101.455Å b: 101.455Å c: 178.728Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Proline mechanisms of stress survival.
Liang et al. (2013)
9 more

3 mentions without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
2 more