› 5c33

X-ray diffraction
1.21Å resolution

Crystal Structure of Mouse Ryanodine Receptor 2 SPRY1 Domain

Released:
DOI: 10.2210/pdb5c33/pdb
PDB entry 5c33 coloured by chain, front view.
PDB entry 5c33 coloured by chain, side view.
PDB entry 5c33 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structures of ryanodine receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant.
Yuchi Z, Yuen SM, Lau K, Underhill AQ, Cornea RL, Fessenden JD, Van Petegem F
Nat Commun 6 7947 (2015)
PMID: 26245150

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 22.09 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9Q401 (Residues: 650-844; Coverage: 4%)
Gene name: Ryr2
Sequence domains: SPRY domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand IPA 2 x IPA
Ligand CL 1 x CL
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 53.246Å b: 64.085Å c: 109.769Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.172
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

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

7 mentions without citation

Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery.
Vénien-Bryan et al. (2017)
6 more