› 1vrk

X-ray diffraction
1.9Å resolution

THE 1.9 ANGSTROM STRUCTURE OF E84K-CALMODULIN RS20 PEPTIDE COMPLEX

Released:
DOI: 10.2210/pdb1vrk/pdb
PDB entry 1vrk coloured by chain, front view.
PDB entry 1vrk coloured by chain, side view.
PDB entry 1vrk coloured by chain, top view.
Source organisms:
Primary publication:
Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties.
Mirzoeva S, Weigand S, Lukas TJ, Shuvalova L, Anderson WF, Watterson DM
Biochemistry 38 3936-47 (1999)
PMID: 10194305

Function and Biology Details

Reaction catalysed: 
ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145928 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CALMODULIN Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.64 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: EF-hand
Myosin light chain kinase, smooth muscle, deglutamylated form Chain: B
Molecule details ›
Chain: B
Length: 21 amino acids
Theoretical weight: 2.33 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: P11799 (Residues: 1731-1749; Coverage: 1%)
Gene name: Mylk

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand ACT 1 x ACT
1 modified residue:
Ligand TRF 1 x TRF

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 61.209Å b: 40.56Å c: 32.774Å
α: 90° β: 91.7° γ: 90°
R-values:
R R work R free
0.171 0.171 0.242
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Novel aspects of calmodulin target recognition and activation.
Vetter et al. (2003)
2 more

4 mentions without citation

Calcium-regulated mitochondrial ATP-Mg/Pi carriers evolved from a fusion of an EF-hand regulatory domain with a mitochondrial ADP/ATP carrier-like domain.
Harborne et al. (2018)
3 more