8sez

Cryo-EM Structure of RyR1 + Adenine (Local Refinement of TMD)

Method: ELECTRON MICROSCOPY Dmax: 144.4 Å Quality: GOOD

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

Ryanodine receptor 1

OrganismNot specified

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 ADE ADENINE × 4 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 8sez

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sez
Deposition date deposition_date2023-04-10
Structure title titleCryo-EM Structure of RyR1 + Adenine (Local Refinement of TMD)
Keywords keywordsCalcium ion channel, skeletal muscle, nucleotide, homotetramer, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.76
Radius of gyration Rg (electron density) rg_electron47.10
Forward intensity I(0) i01140830000.00
Molecular weight molecular_weight292410.0 kDa
Excluded volume excluded_volume369870 ų
Envelope volume envelope_volume563160 ų
Hydration-shell volume shell_volume95483 ų
Envelope diameter envelope_diameter150.2
Shell Rg shell_rg55.08
Envelope Rg envelope_rg46.25
Shape Rg shape_rg47.07
Total Rg total_rg47.49
Total atoms total_atoms20580
Residues n_residues2508
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 dmax144.4
Rg (real space) rg_real47.38
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real1.1410e+09
I(0) uncertainty (real space) i0_real_error2.1260e+07
Rg (reciprocal space) rg_reciprocal47.75
I(0) (reciprocal space) i0_reciprocal1141000000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.9
Skewness Skewness skewness0.083
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105400000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.758

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)