7u9t

Structure of PKA phosphorylated human RyR2 in the closed state in the presence of Calmodulin

Method: ELECTRON MICROSCOPY Dmax: 270.8 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 × 12 PDB declaration: dodecameric(12) 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) Calmodulin-1 × 4 (P0DP23) ZN ZINC ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Xanthine was made fresh to avoid aggregation. Xanthine stock solution was 10 mM in NaOH 0.5 N. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.68 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 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

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 × 12 PDB declaration: dodecameric(12) 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) Calmodulin-1 × 4 (P0DP23) ZN ZINC ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Xanthine was made fresh to avoid aggregation. Xanthine stock solution was 10 mM in NaOH 0.5 N. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.68 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 2
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

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 I; UniProt 1–149 Chain J; UniProt 1–149 Chain K; UniProt 1–149 Chain L; UniProt 1–149 Not recorded Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) Ryanodine receptor 2 × 4 (Q92736) ZN ZINC ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Xanthine was made fresh to avoid aggregation. Xanthine stock solution was 10 mM in NaOH 0.5 N. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.68 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 I; PDBConstruct 1–149; UniProt 1–149 Author chain J; PDBConstruct 1–149; UniProt 1–149 Author chain K; 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 7u9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7u9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7u9t
Deposition date deposition_date2022-03-11
Structure title titleStructure of PKA phosphorylated human RyR2 in the closed state in the presence of Calmodulin
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_electron104.10
Forward intensity I(0) i056278600000.00
Molecular weight molecular_weight2038700.0 kDa
Excluded volume excluded_volume2553500 ų
Envelope volume envelope_volume4711700 ų
Hydration-shell volume shell_volume367670 ų
Envelope diameter envelope_diameter371.4
Shell Rg shell_rg105.80
Envelope Rg envelope_rg100.70
Shape Rg shape_rg104.10
Total Rg total_rg104.10
Total atoms total_atoms143204
Residues n_residues17912
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 dmax270.8
Rg (real space) rg_real100.20
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real5.3770e+10
I(0) uncertainty (real space) i0_real_error9.3870e+08
Rg (reciprocal space) rg_reciprocal104.70
I(0) (reciprocal space) i0_reciprocal56320000000.0000
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_primary126.4
Skewness Skewness skewness0.111
Kurtosis Kurtosis kurtosis-0.666
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7790
Highest regularization parameter α highest_alpha4338000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.999; Stabil: 0.959; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; 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)