5tb0

Structure of rabbit RyR1 (EGTA-only dataset, all particles)

Method: ELECTRON MICROSCOPY Dmax: 272.6 Å Quality: EXCELLENT

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

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 A; UniProt 1–108 Chain F; UniProt 1–108 Chain H; UniProt 1–108 Chain J; UniProt 1–108 Not recorded Ryanodine receptor 1 × 4 (P11716) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 3-4 seconds on both sides with Whatman ashless filter paper, blot force 3, wait time 30 seconds Resolution 4.40 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–108; UniProt 1–108 Author chain F; PDBConstruct 1–108; UniProt 1–108 Author chain H; PDBConstruct 1–108; UniProt 1–108 Author chain J; PDBConstruct 1–108; UniProt 1–108

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 4541–5037 Chain B; UniProt 12–1275 Chain B; UniProt 1573–2479 Chain B; UniProt 2734–2939 Chain B; UniProt 3639–4253 Chain E; UniProt 4541–5037 Chain E; UniProt 12–1275 Chain E; UniProt 1573–2479 Chain E; UniProt 2734–2939 Chain E; UniProt 3639–4253 Chain G; UniProt 4541–5037 Chain G; UniProt 12–1275 Chain G; UniProt 1573–2479 Chain G; UniProt 2734–2939 Chain G; UniProt 3639–4253 Chain I; UniProt 4541–5037 Chain I; UniProt 12–1275 Chain I; UniProt 1573–2479 Chain I; UniProt 2734–2939 Chain I; UniProt 3639–4253 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;Blotted for 3-4 seconds on both sides with Whatman ashless filter paper, blot force 3, wait time 30 seconds Resolution 4.40 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 2
Chains and sequence ranges Author chain B; PDBConstruct 3920–4416; UniProt 4541–5037 Author chain B; PDBConstruct 1–1264; UniProt 12–1275 Author chain B; PDBConstruct 1422–2328; UniProt 1573–2479 Author chain B; PDBConstruct 2546–2751; UniProt 2734–2939 Author chain B; PDBConstruct 3278–3892; UniProt 3639–4253 Author chain E; PDBConstruct 3920–4416; UniProt 4541–5037 Author chain E; PDBConstruct 1–1264; UniProt 12–1275 Author chain E; PDBConstruct 1422–2328; UniProt 1573–2479 Author chain E; PDBConstruct 2546–2751; UniProt 2734–2939 Author chain E; PDBConstruct 3278–3892; UniProt 3639–4253 Author chain G; PDBConstruct 3920–4416; UniProt 4541–5037 Author chain G; PDBConstruct 1–1264; UniProt 12–1275 Author chain G; PDBConstruct 1422–2328; UniProt 1573–2479 Author chain G; PDBConstruct 2546–2751; UniProt 2734–2939 Author chain G; PDBConstruct 3278–3892; UniProt 3639–4253 Author chain I; PDBConstruct 3920–4416; UniProt 4541–5037 Author chain I; PDBConstruct 1–1264; UniProt 12–1275 Author chain I; PDBConstruct 1422–2328; UniProt 1573–2479 Author chain I; PDBConstruct 2546–2751; UniProt 2734–2939 Author chain I; PDBConstruct 3278–3892; UniProt 3639–4253

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 5tb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5tb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5tb0
Deposition date deposition_date2016-09-10
Structure title titleStructure of rabbit RyR1 (EGTA-only dataset, all particles)
Keywords keywordsRyR, Ca2+, EC coupling, gating, TRANSPORT PROTEIN-ISOMERASE complex; TRANSPORT PROTEIN/ISOMERASE
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_electron103.50
Forward intensity I(0) i042267100000.00
Molecular weight molecular_weight1718300.0 kDa
Excluded volume excluded_volume2130600 ų
Envelope volume envelope_volume4686800 ų
Hydration-shell volume shell_volume365900 ų
Envelope diameter envelope_diameter375.5
Shell Rg shell_rg104.70
Envelope Rg envelope_rg101.50
Shape Rg shape_rg103.70
Total Rg total_rg102.90
Total atoms total_atoms121272
Residues n_residues17204
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 dmax272.6
Rg (real space) rg_real100.40
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real4.0320e+10
I(0) uncertainty (real space) i0_real_error7.4080e+08
Rg (reciprocal space) rg_reciprocal104.60
I(0) (reciprocal space) i0_reciprocal42260000000.0000
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_primary127.2
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.654
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.8729
Highest regularization parameter α highest_alpha5191000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.999; Stabil: 0.962; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; 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)