› 8vjj

Electron Microscopy
2.53Å resolution

Structure of mouse RyR1 (EGTA-only dataset)

Released:
DOI: 10.2210/pdb8vjj/pdb
PDB entry 8vjj coloured by chain, front view.
PDB entry 8vjj coloured by chain, side view.
PDB entry 8vjj coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural insights into the regulation of RyR1 by S100A1.
Weninger G, Miotto MC, Tchagou C, Reiken S, Dridi H, Brandenburg S, Riedemann GC, Yuan Q, Liu Y, Chang A, Wronska A, Lehnart SE, Marks AR
Proc Natl Acad Sci U S A 121 e2400497121 (2024)
PMID: 38917010
Related structures: EMD-43283

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-238896 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ryanodine receptor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 5035 amino acids
Theoretical weight: 565.69 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: E9PZQ0 (Residues: 1-5035; Coverage: 100%)
Gene name: Ryr1
Sequence domains:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 108 amino acids
Theoretical weight: 11.94 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P26883 (Residues: 1-108; Coverage: 100%)
Gene names: Fkbp1, Fkbp1a
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand PCW 8 x PCW
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.53Å
Relevant EMDB volumes: EMD-43283

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