8uxi

Structure of PKA phosphorylated human RyR2-R420W in the open state in the presence of calcium

Method: ELECTRON MICROSCOPY Dmax: 267.9 Å Quality: EXCELLENT

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

Ryanodine receptor 2

Homo sapiens

UniProt Q92736

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 1–4967 Chain B; UniProt 1–4967 Chain C; UniProt 1–4967 Chain D; UniProt 1–4967 Not recorded Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) ZN ZINC ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RYR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–4967; UniProt 1–4967 Author chain B; PDBConstruct 1–4967; UniProt 1–4967 Author chain C; PDBConstruct 1–4967; UniProt 1–4967 Author chain D; PDBConstruct 1–4967; UniProt 1–4967

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 E; UniProt 1–108 Chain F; UniProt 1–108 Chain G; UniProt 1–108 Chain H; UniProt 1–108 Not recorded Ryanodine receptor 2 × 4 (Q92736) ZN ZINC ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 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 1–108; UniProt 1–108 Author chain F; PDBConstruct 1–108; UniProt 1–108 Author chain G; PDBConstruct 1–108; UniProt 1–108 Author chain H; PDBConstruct 1–108; UniProt 1–108

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 8uxi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8uxi
Deposition date deposition_date2023-11-09
Structure title titleStructure of PKA phosphorylated human RyR2-R420W in the open state in the presence of calcium
Keywords keywordscalcium channel, 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_electron103.10
Forward intensity I(0) i047407300000.00
Molecular weight molecular_weight1873200.0 kDa
Excluded volume excluded_volume2347200 ų
Envelope volume envelope_volume4372100 ų
Hydration-shell volume shell_volume348700 ų
Envelope diameter envelope_diameter375.3
Shell Rg shell_rg103.10
Envelope Rg envelope_rg99.30
Shape Rg shape_rg103.10
Total Rg total_rg103.00
Total atoms total_atoms131624
Residues n_residues16444
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 dmax267.9
Rg (real space) rg_real99.13
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real4.5290e+10
I(0) uncertainty (real space) i0_real_error8.9810e+08
Rg (reciprocal space) rg_reciprocal103.60
I(0) (reciprocal space) i0_reciprocal47440000000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary125.0
Skewness Skewness skewness0.109
Kurtosis Kurtosis kurtosis-0.657
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7978
Highest regularization parameter α highest_alpha3811000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.998; Stabil: 0.963; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)