8x4e

Cryo-EM structure of Ryanodine receptor 1 (TM helix S0, 5 mM Ca2+)

Method: ELECTRON MICROSCOPY Dmax: 263.0 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ryanodine receptor 1

Oryctolagus cuniculus

UniProt P11716

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–5037 Chain B; UniProt 1–5037 Chain C; UniProt 1–5037 Chain D; UniProt 1–5037 Not recorded ZN ZINC ION × 4 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

124 other PDB entries and 135 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RYR1_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–5037; UniProt 1–5037 Author chain B; PDBConstruct 1–5037; UniProt 1–5037 Author chain C; PDBConstruct 1–5037; UniProt 1–5037 Author chain D; PDBConstruct 1–5037; UniProt 1–5037

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8x4e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x4e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x4e
Deposition date deposition_date2023-11-15
Structure title titleCryo-EM structure of Ryanodine receptor 1 (TM helix S0, 5 mM Ca2+)
Keywords keywordsRyanodine Receptor, Calcium release channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron100.40
Forward intensity I(0) i038862300000.00
Molecular weight molecular_weight1680000.0 kDa
Excluded volume excluded_volume2098100 ų
Envelope volume envelope_volume4303400 ų
Hydration-shell volume shell_volume347440 ų
Envelope diameter envelope_diameter376.1
Shell Rg shell_rg100.70
Envelope Rg envelope_rg99.76
Shape Rg shape_rg100.50
Total Rg total_rg100.20
Total atoms total_atoms118280
Residues n_residues15928
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax263.0
Rg (real space) rg_real96.29
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real3.7100e+10
I(0) uncertainty (real space) i0_real_error6.6900e+08
Rg (reciprocal space) rg_reciprocal100.50
I(0) (reciprocal space) i0_reciprocal38820000000.0000
Solution quality estimate total_estimate0.9116
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary122.7
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7195
Highest regularization parameter α highest_alpha4654000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 1.000; Stabil: 0.969; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)