› 1bg0

X-ray diffraction
1.86Å resolution

TRANSITION STATE STRUCTURE OF ARGININE KINASE

Released:
DOI: 10.2210/pdb1bg0/pdb
PDB entry 1bg0 coloured by chain, front view.
PDB entry 1bg0 coloured by chain, side view.
PDB entry 1bg0 coloured by chain, top view.
Source organism: Limulus polyphemus
Primary publication:
Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS
Proc Natl Acad Sci U S A 95 8449-54 (1998)
PMID: 9671698

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: 356 amino acids
Theoretical weight: 40.12 KDa
Source organism: Limulus polyphemus
Expression system: Escherichia coli
UniProt:
  • Canonical: P51541 (Residues: 2-357; 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 RUH2R
Spacegroup: P212121
Unit cell:
a: 65.439Å b: 70.885Å c: 80.437Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
3 more

14 mentions without citation

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