6ofj

Cryo-EM structure of the native rhodopsin dimer from rod photoreceptor cells

Method: ELECTRON MICROSCOPY Dmax: 98.9 Å Quality: EXCELLENT

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

Rhodopsin

OrganismNot specified

UniProt P02699

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–348 Chain B; UniProt 1–348 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

74 other PDB entries and 95 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPSD_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–348; UniProt 1–348 Author chain B; PDBConstruct 1–348; UniProt 1–348

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 6ofj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ofj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ofj
Deposition date deposition_date2019-03-30
Structure title titleCryo-EM structure of the native rhodopsin dimer from rod photoreceptor cells
Keywords keywordsG protein-coupled receptor, native dimer, rod outer segment, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.13
Radius of gyration Rg (electron density) rg_electron29.91
Forward intensity I(0) i073435400.00
Molecular weight molecular_weight73379.0 kDa
Excluded volume excluded_volume94164 ų
Envelope volume envelope_volume124400 ų
Hydration-shell volume shell_volume34480 ų
Envelope diameter envelope_diameter95.7
Shell Rg shell_rg37.36
Envelope Rg envelope_rg29.55
Shape Rg shape_rg29.91
Total Rg total_rg30.66
Total atoms total_atoms10310
Residues n_residues650
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 dmax98.9
Rg (real space) rg_real31.04
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real7.3440e+07
I(0) uncertainty (real space) i0_real_error1.1060e+06
Rg (reciprocal space) rg_reciprocal31.08
I(0) (reciprocal space) i0_reciprocal73440000.0000
Solution quality estimate total_estimate0.9031
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.682
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28230000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)