6rqo

Steady-state-SMX activated state structure of bacteriorhodopsin

Method: X-RAY DIFFRACTION Dmax: 61.3 Å Quality: GOOD

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 18–240 Not recorded RET RETINAL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 5.6;294 K;100 mM Na/K Phosphate buffer pH 5.6 30 % PEG 2000 Resolution 2.00 Å R-free 0.246

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 1–223; UniProt 18–240

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 6rqo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6rqo
Deposition date deposition_date2019-05-16
Structure title titleSteady-state-SMX activated state structure of bacteriorhodopsin
Keywords keywordsretinal, serial crystallography, time-resolved crystallography, TR-SMX, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.01
Radius of gyration Rg (electron density) rg_electron17.89
Forward intensity I(0) i08208660.00
Molecular weight molecular_weight24536.0 kDa
Excluded volume excluded_volume32128 ų
Envelope volume envelope_volume34793 ų
Hydration-shell volume shell_volume16587 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg23.76
Envelope Rg envelope_rg18.29
Shape Rg shape_rg17.87
Total Rg total_rg18.98
Total atoms total_atoms1736
Residues n_residues223
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 dmax61.3
Rg (real space) rg_real19.02
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real8.2090e+06
I(0) uncertainty (real space) i0_real_error1.0000e+05
Rg (reciprocal space) rg_reciprocal19.02
I(0) (reciprocal space) i0_reciprocal8209000.0000
Solution quality estimate total_estimate0.8160
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1800000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; 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_idd6rqoa_
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_id6rqoA00
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)