5te5

Crystal structure of Bos taurus opsin regenerated with 6-carbon ring retinal chromophore

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–348 Non-standard monomer:Yes (specific site not provided by mmCIF) 7AB (2E)-{(4E)-4-[(3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-ylidene]cyclohex-2-en-1-ylidene}acetaldehyde × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;2.8-3.4 M ammonium sulfate in 0.05-0.1 M MES, pH 6.1-6.6, or 0.05-0.1 M NaAcO buffer, pH 5.2-5.6 Resolution 4.01 Å R-free 0.357

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 5te5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5te5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5te5
Deposition date deposition_date2016-09-20
Structure title titleCrystal structure of Bos taurus opsin regenerated with 6-carbon ring retinal chromophore
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.79
Radius of gyration Rg (electron density) rg_electron22.45
Forward intensity I(0) i022625100.00
Molecular weight molecular_weight39327.0 kDa
Excluded volume excluded_volume50416 ų
Envelope volume envelope_volume58864 ų
Hydration-shell volume shell_volume22340 ų
Envelope diameter envelope_diameter82.9
Shell Rg shell_rg29.17
Envelope Rg envelope_rg23.05
Shape Rg shape_rg22.44
Total Rg total_rg23.43
Total atoms total_atoms2770
Residues n_residues348
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 dmax78.8
Rg (real space) rg_real23.89
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real2.2630e+07
I(0) uncertainty (real space) i0_real_error2.9600e+05
Rg (reciprocal space) rg_reciprocal23.87
I(0) (reciprocal space) i0_reciprocal22620000.0000
Solution quality estimate total_estimate0.7927
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5590000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)