› 3m10

X-ray diffraction
1.73Å resolution

Substrate-free form of Arginine Kinase

Released:
DOI: 10.2210/pdb3m10/pdb
PDB entry 3m10 coloured by chain, front view.
PDB entry 3m10 coloured by chain, side view.
PDB entry 3m10 coloured by chain, top view.
Source organism: Limulus polyphemus
Primary publication:
Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.
Niu X, Bruschweiler-Li L, Davulcu O, Skalicky JJ, Brüschweiler R, Chapman MS
J Mol Biol 405 479-96 (2011)
PMID: 21075117

Function and Biology Details

Reaction catalysed: 
ATP + L-arginine = ADP + N(omega)-phospho-L-arginine
Biochemical function:
Biological process:
Cellular component:
Sequence 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 Chains: A, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 60.218Å b: 90.428Å c: 70.554Å
α: 90° β: 111.02° γ: 90°
R-values:
R R work R free
0.192 0.19 0.242
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein dynamics and function from solution state NMR spectroscopy.
Kovermann et al. (2016)
1 more

8 mentions without citation

Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.
Niu et al. (2011)
7 more