6fk9

Crystal structure of N2C/D282C stabilized opsin bound to RS09

Method: X-RAY DIFFRACTION Dmax: 90.0 Å Quality: GOOD

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

Rhodopsin

Bos taurus

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–348 Fragment:RESIDUES 1-326 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 PLM PALMITIC ACID × 1 BOG octyl beta-D-glucopyranoside × 4 DNK (2~{S})-3-methyl-2-phenyl-1-spiro[1,3-benzodioxole-2,4'-piperidine]-1'-yl-butan-1-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;see publication Resolution 2.63 Å R-free 0.261

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 2–349; 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 6fk9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fk9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6fk9
Deposition date deposition_date2018-01-23
Structure title titleCrystal structure of N2C/D282C stabilized opsin bound to RS09
Keywords keywords;RHODOPSIN, G PROTEIN-COUPLED RECEPTORS, RETINITIS PIGMENTOSA, SIGNALING PROTEIN, SENSORY TRANSDUCTION, PHOTORECEPTOR PROTEIN, KINTEGRAL MEMBRANE PROTEIN, VISION, MEMBRANE, RECEPTOR, TRANSDUCER PHOTORECEPTOR, SMALL MOLECULE COMPLEX, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.87
Radius of gyration Rg (electron density) rg_electron22.58
Forward intensity I(0) i021734800.00
Molecular weight molecular_weight39483.0 kDa
Excluded volume excluded_volume51003 ų
Envelope volume envelope_volume60109 ų
Hydration-shell volume shell_volume22749 ų
Envelope diameter envelope_diameter93.2
Shell Rg shell_rg29.03
Envelope Rg envelope_rg23.52
Shape Rg shape_rg22.52
Total Rg total_rg23.68
Total atoms total_atoms2775
Residues n_residues326
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 dmax90.0
Rg (real space) rg_real24.03
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real2.1730e+07
I(0) uncertainty (real space) i0_real_error2.9490e+05
Rg (reciprocal space) rg_reciprocal23.99
I(0) (reciprocal space) i0_reciprocal21730000.0000
Solution quality estimate total_estimate0.8017
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.537
Kurtosis Kurtosis kurtosis-0.054
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3357000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.599; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.647; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6fk9a_
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 (1 domains)

Domain ID domain_id6fk9A00
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)