4ov0

Structure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase

Method: X-RAY DIFFRACTION Dmax: 62.7 Å Quality: REASONABLE

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

Bacteriorhodopsin

OrganismNot specified

UniProt P02945

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–262 Not recorded RET RETINAL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;295 K;Monooleoyl, amphipol A8-35, 1-2M sodium/potassium phosphate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.00 Å R-free 0.209

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.

173 other PDB entries and 201 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BACR_HALSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–249; UniProt 14–262

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 4ov0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ov0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ov0
Deposition date deposition_date2014-02-19
Structure title titleStructure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase
Keywords keywordsLight-driven proton pump, Retinal attached via Schiff base, Membrane, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.51
Radius of gyration Rg (electron density) rg_electron17.41
Forward intensity I(0) i07643580.00
Molecular weight molecular_weight23749.0 kDa
Excluded volume excluded_volume31157 ų
Envelope volume envelope_volume33372 ų
Hydration-shell volume shell_volume16262 ų
Envelope diameter envelope_diameter64.4
Shell Rg shell_rg23.44
Envelope Rg envelope_rg17.90
Shape Rg shape_rg17.39
Total Rg total_rg18.57
Total atoms total_atoms1681
Residues n_residues214
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 dmax62.7
Rg (real space) rg_real18.52
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real7.6440e+06
I(0) uncertainty (real space) i0_real_error8.9640e+04
Rg (reciprocal space) rg_reciprocal18.52
I(0) (reciprocal space) i0_reciprocal7644000.0000
Solution quality estimate total_estimate0.6529
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1659000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 1.000; Sysdev: 0.391; Positv: 1.000; Valcen: 0.969; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4ov0a_
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.13.1.1 — Bacteriorhodopsin-like

CATH v4.4 (1 domains)

Domain ID domain_id4ov0A00
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)