› 1m15

X-ray diffraction
1.2Å resolution

Transition state structure of arginine kinase

Released:
DOI: 10.2210/pdb1m15/pdb
PDB entry 1m15 coloured by chain, front view.
PDB entry 1m15 coloured by chain, side view.
PDB entry 1m15 coloured by chain, top view.
Source organism: Limulus polyphemus
Primary publication:
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS
Acta Crystallogr D Biol Crystallogr 58 2009-17 (2002)
PMID: 12454458

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: 40.25 KDa
Source organism: Limulus polyphemus
Expression system: Escherichia coli
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 ARG 1 x ARG
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 65.393Å b: 70.312Å c: 80.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 0.125 0.14
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Relating structure to mechanism in creatine kinase.
McLeish et al. (2005)
2 more

18 mentions without citation

Evolutionarily conserved amino acids that control TCR-MHC interaction.
Marrack et al. (2008)
17 more