3cap

Crystal Structure of Native Opsin: the G Protein-Coupled Receptor Rhodopsin in its Ligand-free State

Method: X-RAY DIFFRACTION Dmax: 96.9 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 Other combination Homooligomer Protein × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–348 Chain B; UniProt 1–348 Not recorded ;beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 BGL 2-O-octyl-beta-D-glucopyranose × 6 PLM PALMITIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;AMMONIUM SULFATE, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.266

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 3cap

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3cap
Deposition date deposition_date2008-02-20
Structure title titleCrystal Structure of Native Opsin: the G Protein-Coupled Receptor Rhodopsin in its Ligand-free State
Keywords keywords;G PROTEIN-COUPLED RECEPTOR, OPSIN, RHODOPSIN, MEMBRANE PROTEIN, RETINAL PROTEIN, PHOTORECEPTOR, LIGAND-FREE STATE, Chromophore, G-protein coupled receptor, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Photoreceptor protein, Sensory transduction, Transducer, Transmembrane, Vision, 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_guinier30.78
Radius of gyration Rg (electron density) rg_electron29.32
Forward intensity I(0) i081246100.00
Molecular weight molecular_weight78126.0 kDa
Excluded volume excluded_volume100650 ų
Envelope volume envelope_volume125980 ų
Hydration-shell volume shell_volume35335 ų
Envelope diameter envelope_diameter102.7
Shell Rg shell_rg36.94
Envelope Rg envelope_rg29.46
Shape Rg shape_rg29.33
Total Rg total_rg30.09
Total atoms total_atoms5494
Residues n_residues652
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 dmax96.9
Rg (real space) rg_real30.69
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real8.1250e+07
I(0) uncertainty (real space) i0_real_error1.2160e+06
Rg (reciprocal space) rg_reciprocal30.73
I(0) (reciprocal space) i0_reciprocal81250000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary95.0
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.592
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13930000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3capa_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamilyf.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family familyf.13.1.2 — Rhodopsin-like
Domain ID domain_idd3capb_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamilyf.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family familyf.13.1.2 — Rhodopsin-like

CATH v4.4 (2 domains)

Domain ID domain_id3capA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins
Domain ID domain_id3capB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)