› 1p52

X-ray diffraction
1.9Å resolution

Structure of Arginine kinase E314D mutant

Released:
DOI: 10.2210/pdb1p52/pdb
PDB entry 1p52 coloured by chain, front view.
PDB entry 1p52 coloured by chain, side view.
PDB entry 1p52 coloured by chain, top view.
Source organism: Limulus polyphemus
Primary publication:
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
Pruett PS, Azzi A, Clark SA, Yousef MS, Gattis JL, Somasundaram T, Ellington WR, Chapman MS
J Biol Chem 278 26952-7 (2003)
PMID: 12732621

Function and Biology Details

Reaction catalysed: 
ATP + L-arginine = ADP + N(omega)-phospho-L-arginine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156357 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine kinase Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 40.29 KDa
Source organism: Limulus polyphemus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51541 (Residues: 1-357; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand NO3 2 x NO3
Ligand MG 1 x MG
Ligand ADP 1 x ADP
Ligand DAR 1 x DAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 65.393Å b: 70.312Å c: 80.139Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
1 more

5 mentions without citation

A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis.
Kirstein et al. (2005)
4 more