8dve

RyR1 in presence of IpCa-T26E phosphomimetic and activating ligands

Method: ELECTRON MICROSCOPY Dmax: 255.8 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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–5037 Chain D; UniProt 1–5037 Chain G; UniProt 1–5037 Chain J; UniProt 1–5037 Not recorded Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) Calmodulin-1 × 4 (P0DP23) CFF CAFFEINE × 4 CA CALCIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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 D; PDBConstruct 1–5037; UniProt 1–5037 Author chain G; PDBConstruct 1–5037; UniProt 1–5037 Author chain J; PDBConstruct 1–5037; UniProt 1–5037

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 2–108 Chain E; UniProt 2–108 Chain H; UniProt 2–108 Chain K; UniProt 2–108 Not recorded Ryanodine receptor 1 × 4 (P11716) Calmodulin-1 × 4 (P0DP23) CFF CAFFEINE × 4 CA CALCIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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 B; PDBConstruct 1–107; UniProt 2–108 Author chain E; PDBConstruct 1–107; UniProt 2–108 Author chain H; PDBConstruct 1–107; UniProt 2–108 Author chain K; PDBConstruct 1–107; UniProt 2–108

Calmodulin-1

Homo sapiens

UniProt P0DP23

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–149 Chain F; UniProt 1–149 Chain I; UniProt 1–149 Chain L; UniProt 1–149 Mutation:E32A, E68A, E105A, E141A Ryanodine receptor 1 × 4 (P11716) Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) CFF CAFFEINE × 4 CA CALCIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–149; UniProt 1–149 Author chain F; PDBConstruct 1–149; UniProt 1–149 Author chain I; PDBConstruct 1–149; UniProt 1–149 Author chain L; PDBConstruct 1–149; UniProt 1–149

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 8dve

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8dve
Deposition date deposition_date2022-07-28
Structure title titleRyR1 in presence of IpCa-T26E phosphomimetic and activating ligands
Keywords keywordsRyanodine receptor, Ion channel, Snake toxin, Calcin, Complex, 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_electron99.12
Forward intensity I(0) i035955500000.00
Molecular weight molecular_weight1615100.0 kDa
Excluded volume excluded_volume2014200 ų
Envelope volume envelope_volume4232000 ų
Hydration-shell volume shell_volume341800 ų
Envelope diameter envelope_diameter357.8
Shell Rg shell_rg102.00
Envelope Rg envelope_rg97.43
Shape Rg shape_rg99.34
Total Rg total_rg98.36
Total atoms total_atoms114229
Residues n_residues16751
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 dmax255.8
Rg (real space) rg_real96.72
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real3.4470e+10
I(0) uncertainty (real space) i0_real_error6.6570e+08
Rg (reciprocal space) rg_reciprocal101.10
I(0) (reciprocal space) i0_reciprocal36020000000.0000
Solution quality estimate total_estimate0.9146
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary111.9
Skewness Skewness skewness0.111
Kurtosis Kurtosis kurtosis-0.673
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.4708
Highest regularization parameter α highest_alpha4797000000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 1.000; Stabil: 0.965; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)