8sen

Cryo-EM Structure of RyR1

Method: ELECTRON MICROSCOPY Dmax: 273.4 Å Quality: EXCELLENT

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 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) 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 Glutathione S-transferase class-mu 26 kDa isozyme,Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P08515,P68106) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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

Glutathione S-transferase class-mu 26 kDa isozyme,Peptidyl-prolyl cis-trans isomerase FKBP1B

Homo sapiens

UniProt P08515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–218 Chain F; UniProt 1–218 Chain G; UniProt 1–218 Chain H; UniProt 1–218 Not recorded Ryanodine receptor 1 × 4 (P11716) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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.

64 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GST26_SCHJA
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 14–231; UniProt 1–218 Author chain F; PDBConstruct 14–231; UniProt 1–218 Author chain G; PDBConstruct 14–231; UniProt 1–218 Author chain H; PDBConstruct 14–231; UniProt 1–218

Glutathione S-transferase class-mu 26 kDa isozyme,Peptidyl-prolyl cis-trans isomerase FKBP1B

Homo sapiens

UniProt P68106

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 2–108 Chain F; UniProt 2–108 Chain G; UniProt 2–108 Chain H; UniProt 2–108 Not recorded Ryanodine receptor 1 × 4 (P11716) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 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.

117 other PDB entries and 119 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FKB1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 244–350; UniProt 2–108 Author chain F; PDBConstruct 244–350; UniProt 2–108 Author chain G; PDBConstruct 244–350; UniProt 2–108 Author chain H; PDBConstruct 244–350; UniProt 2–108

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 8sen

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sen
Deposition date deposition_date2023-04-10
Structure title titleCryo-EM Structure of RyR1
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_guinier
Radius of gyration Rg (electron density) rg_electron105.20
Forward intensity I(0) i055841300000.00
Molecular weight molecular_weight2030200.0 kDa
Excluded volume excluded_volume2543000 ų
Envelope volume envelope_volume4710600 ų
Hydration-shell volume shell_volume365690 ų
Envelope diameter envelope_diameter372.0
Shell Rg shell_rg105.70
Envelope Rg envelope_rg101.40
Shape Rg shape_rg105.20
Total Rg total_rg105.10
Total atoms total_atoms142708
Residues n_residues17940
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 dmax273.4
Rg (real space) rg_real101.40
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real5.3360e+10
I(0) uncertainty (real space) i0_real_error9.7740e+08
Rg (reciprocal space) rg_reciprocal105.80
I(0) (reciprocal space) i0_reciprocal55880000000.0000
Solution quality estimate total_estimate0.9097
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary127.6
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.693
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.8028
Highest regularization parameter α highest_alpha5658000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.958; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; 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)