3ila

Crystal structure of rabbit ryanodine receptor 1 N-terminal domain (9-205)

Method: X-RAY DIFFRACTION Dmax: 113.6 Å Quality: GOOD

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

Ryanodine receptor 1

Oryctolagus cuniculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 9–205 Fragment:N-Terminal Domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;15-25% PEG 3350, 0.2M sodium chloride, 0.1M BisTris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.320

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 127 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 1–197; UniProt 9–205 Author chain B; PDBConstruct 1–197; UniProt 9–205 Author chain C; PDBConstruct 1–197; UniProt 9–205 Author chain D; PDBConstruct 1–197; UniProt 9–205 Author chain E; PDBConstruct 1–197; UniProt 9–205 Author chain F; PDBConstruct 1–197; UniProt 9–205 Author chain G; PDBConstruct 1–197; UniProt 9–205 Author chain H; PDBConstruct 1–197; UniProt 9–205 Author chain I; PDBConstruct 1–197; UniProt 9–205

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 3ila

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ila
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ila
Deposition date deposition_date2009-08-06
Structure title titleCrystal structure of rabbit ryanodine receptor 1 N-terminal domain (9-205)
Keywords keywords;BETA TREFOIL, Calcium channel, Calcium transport, Glycoprotein, Ion transport, Ionic channel, Membrane, Phosphoprotein, Receptor, S-nitrosylation, Transmembrane, Transport, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.56
Radius of gyration Rg (electron density) rg_electron36.71
Forward intensity I(0) i0320254000.00
Molecular weight molecular_weight141730.0 kDa
Excluded volume excluded_volume176040 ų
Envelope volume envelope_volume262360 ų
Hydration-shell volume shell_volume58952 ų
Envelope diameter envelope_diameter122.1
Shell Rg shell_rg43.59
Envelope Rg envelope_rg35.71
Shape Rg shape_rg36.71
Total Rg total_rg37.18
Total atoms total_atoms9944
Residues n_residues1394
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 dmax113.6
Rg (real space) rg_real37.27
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real3.2030e+08
I(0) uncertainty (real space) i0_real_error5.2520e+06
Rg (reciprocal space) rg_reciprocal37.45
I(0) (reciprocal space) i0_reciprocal320300000.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36540000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3ilaa_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilab_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilac_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilad_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilae_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilaf_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilag_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like
Domain ID domain_idd3ilah_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.6 — MIR domain
Family Family familyb.42.6.2 — Ryanodine receptor N-terminal-like

CATH v4.4 (8 domains)

Domain ID domain_id3ilaA00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaB00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaC00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaD00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaE00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaF00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaG00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3ilaH00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50

8. Citations (1)

9. Files and Curves (10)