› 2mc2

Solution NMR

X-ray crystallography-solution NMR hybrid structure of mouse RyR2 domain A

Released:
DOI: 10.2210/pdb2mc2/pdb
PDB entry 2mc2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2mc2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2mc2 coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Type 2 ryanodine receptor domain A contains a unique and dynamic α-helix that transitions to a β-strand in a mutant linked with a heritable cardiomyopathy.
Amador FJ, Kimlicka L, Stathopulos PB, Gasmi-Seabrook GM, Maclennan DH, Van Petegem F, Ikura M
J Mol Biol 425 4034-46 (2013)
PMID: 23978697

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ryanodine receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.17 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: E9Q401 (Residues: 10-224; Coverage: 4%)
Gene name: Ryr2
Sequence domains: Inositol 1,4,5-trisphosphate/ryanodine receptor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 32%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Ryanodine receptors: allosteric ion channel giants.
Van Petegem F. (2015)
4 more