› 5l1d

Electron Microscopy
11Å resolution

Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)

Released:
DOI: 10.2210/pdb5l1d/pdb
PDB entry 5l1d coloured by chain, front view.
PDB entry 5l1d coloured by chain, side view.
PDB entry 5l1d coloured by chain, top view.
Source organisms:
Primary publication:
A cryo-EM-based model of phosphorylation- and FKBP12.6-mediated allosterism of the cardiac ryanodine receptor.
Dhindwal S, Lobo J, Cabra V, Santiago DJ, Nayak AR, Dryden K, Samsó M
Sci Signal 10 (2017)
PMID: 28536302
Related structures: EMD-8303

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159283 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ryanodine Receptor Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 4387 amino acids
Theoretical weight: 487.12 KDa
Source organism: Oryctolagus cuniculus
Peptidyl-prolyl cis-trans isomerase FKBP1B Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 158 amino acids
Theoretical weight: 17.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 11Å
Relevant EMDB volumes: EMD-8303
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

The structural basis of ryanodine receptor ion channel function.
Meissner G. (2017)
5 more

3 mentions without citation

Redox Dependent Modifications of Ryanodine Receptor: Basic Mechanisms and Implications in Heart Diseases.
Nikolaienko et al. (2018)
2 more