7vml

Structure of recombinant RyR2 (EGTA dataset, class 1&2, closed state)

Method: ELECTRON MICROSCOPY Dmax: 267.0 Å Quality: EXCELLENT

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

Ryanodine receptor 2

Mus musculus

UniProt E9Q401

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–1311 Chain A; UniProt 1340–1386 Chain A; UniProt 1566–2507 Chain A; UniProt 2712–2915 Chain A; UniProt 3611–4966 Chain B; UniProt 1–1311 Chain B; UniProt 1340–1386 Chain B; UniProt 1566–2507 Chain B; UniProt 2712–2915 Chain B; UniProt 3611–4966 Chain C; UniProt 1–1311 Chain C; UniProt 1340–1386 Chain C; UniProt 1566–2507 Chain C; UniProt 2712–2915 Chain C; UniProt 3611–4966 Chain D; UniProt 1–1311 Chain D; UniProt 1340–1386 Chain D; UniProt 1566–2507 Chain D; UniProt 2712–2915 Chain D; UniProt 3611–4966 Not recorded Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) ZN ZINC 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.

31 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RYR2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1311; UniProt 1–1311 Author chain A; PDBConstruct 1340–1386; UniProt 1340–1386 Author chain A; PDBConstruct 1566–2507; UniProt 1566–2507 Author chain A; PDBConstruct 2712–2915; UniProt 2712–2915 Author chain A; PDBConstruct 3611–4966; UniProt 3611–4966 Author chain B; PDBConstruct 1–1311; UniProt 1–1311 Author chain B; PDBConstruct 1340–1386; UniProt 1340–1386 Author chain B; PDBConstruct 1566–2507; UniProt 1566–2507 Author chain B; PDBConstruct 2712–2915; UniProt 2712–2915 Author chain B; PDBConstruct 3611–4966; UniProt 3611–4966 Author chain C; PDBConstruct 1–1311; UniProt 1–1311 Author chain C; PDBConstruct 1340–1386; UniProt 1340–1386 Author chain C; PDBConstruct 1566–2507; UniProt 1566–2507 Author chain C; PDBConstruct 2712–2915; UniProt 2712–2915 Author chain C; PDBConstruct 3611–4966; UniProt 3611–4966 Author chain D; PDBConstruct 1–1311; UniProt 1–1311 Author chain D; PDBConstruct 1340–1386; UniProt 1340–1386 Author chain D; PDBConstruct 1566–2507; UniProt 1566–2507 Author chain D; PDBConstruct 2712–2915; UniProt 2712–2915 Author chain D; PDBConstruct 3611–4966; UniProt 3611–4966

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 2–108 Chain H; UniProt 2–108 Chain I; UniProt 2–108 Chain J; UniProt 2–108 Not recorded Ryanodine receptor 2 × 4 (E9Q401) ZN ZINC 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.

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 G; PDBConstruct 70–176; UniProt 2–108 Author chain H; PDBConstruct 70–176; UniProt 2–108 Author chain I; PDBConstruct 70–176; UniProt 2–108 Author chain J; PDBConstruct 70–176; 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 7vml

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7vml
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7vml
Deposition date deposition_date2021-10-09
Structure title titleStructure of recombinant RyR2 (EGTA dataset, class 1&2, closed state)
Keywords keywords;CALCIUM, CALCIUM CHANNEL, CALCIUM TRANSPORT, ION TRANSPORT, IONIC CHANNEL, METAL TRANSPORT, ER/SR MEMBRANE, RYANODINE RECEPTOR, RYANODINE, RECEPTOR, WILD TYPE, 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_electron101.20
Forward intensity I(0) i043502000000.00
Molecular weight molecular_weight1754100.0 kDa
Excluded volume excluded_volume2180400 ų
Envelope volume envelope_volume4427400 ų
Hydration-shell volume shell_volume353280 ų
Envelope diameter envelope_diameter380.4
Shell Rg shell_rg103.40
Envelope Rg envelope_rg99.38
Shape Rg shape_rg101.30
Total Rg total_rg100.80
Total atoms total_atoms123564
Residues n_residues16604
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 dmax267.0
Rg (real space) rg_real98.00
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real4.1490e+10
I(0) uncertainty (real space) i0_real_error7.8710e+08
Rg (reciprocal space) rg_reciprocal102.20
I(0) (reciprocal space) i0_reciprocal43520000000.0000
Solution quality estimate total_estimate0.9101
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary124.6
Skewness Skewness skewness0.137
Kurtosis Kurtosis kurtosis-0.632
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.9277
Highest regularization parameter α highest_alpha5870000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.999; Stabil: 0.963; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; 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)