› 7kl5

X-ray diffraction
1.65Å resolution

Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues: Phe4246 to Val4271

Released:
DOI: 10.2210/pdb7kl5/pdb
PDB entry 7kl5 coloured by chain, front view.
PDB entry 7kl5 coloured by chain, side view.
PDB entry 7kl5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues Phe4246-Val4271 Reveals a Fifth Calcium Binding Site.
Yu Q, Anderson DE, Kaur R, Fisher AJ, Ames JB
Biochemistry 60 1088-1096 (2021)
PMID: 33754699

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143955 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 1-149; Coverage: 100%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Ryanodine receptor 2 Chain: B
Molecule details ›
Chain: B
Length: 30 amino acids
Theoretical weight: 3.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92736 (Residues: 4246-4275; Coverage: 1%)
Gene name: RYR2

Ligands and Environments

2 bound ligands:
Ligand CA 5 x CA
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 33.169Å b: 62.403Å c: 43.19Å
α: 90° β: 107.494° γ: 90°
R-values:
R R work R free
0.211 0.209 0.246
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structural analyses of human ryanodine receptor type 2 channels reveal the mechanisms for sudden cardiac death and treatment.
Miotto et al. (2022)
2 more

2 mentions without citation

Chemical shift assignments of calmodulin under standard conditions at neutral pH.
Bej et al. (2022)
1 more