› 1ahr

X-ray diffraction
1.8Å resolution

CALMODULIN MUTANT WITH A TWO RESIDUE DELETION IN THE CENTRAL HELIX

Released:
DOI: 10.2210/pdb1ahr/pdb
PDB entry 1ahr coloured by chain, front view.
PDB entry 1ahr coloured by chain, side view.
PDB entry 1ahr coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding.
Tabernero L, Taylor DA, Chandross RJ, VanBerkum MF, Means AR, Quiocho FA, Sack JS
Structure 5 613-22 (1997)
PMID: 9195880

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158569 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.48 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62149 (Residues: 2-149; Coverage: 98%)
Gene names: CALM, CAM, RCJMB04_24e7
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 27.09Å b: 55.51Å c: 100.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

3 mentions without citation

Physically realistic homology models built with ROSETTA can be more accurate than their templates.
Misura et al. (2006)
2 more