4x31

Room temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation

Method: X-RAY DIFFRACTION Dmax: 64.0 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 18–246 Fragment:UNP RESIDUES 18-246 RET RETINAL × 3 LI1 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL × 15 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 5.6;294 K;Precipitant: 27%-39% PEG 2000, 100 mM phosphate buffer pH 5.6. MAG 9.9 used for LCP formation. Crystallization setup in Hamilton syringe with tube of LCP surrounded by precipitant. Resolution 2.40 Å R-free 0.249

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 1–229; UniProt 18–246

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 4x31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4x31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4x31
Deposition date deposition_date2014-11-27
Structure title titleRoom temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation
Keywords keywordslight-driven proton pump, seven transmembrane helix protein, room temperature structure, retinal-binding protein, 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_guinier19.26
Radius of gyration Rg (electron density) rg_electron18.21
Forward intensity I(0) i08356750.00
Molecular weight molecular_weight25951.0 kDa
Excluded volume excluded_volume34430 ų
Envelope volume envelope_volume38016 ų
Hydration-shell volume shell_volume17626 ų
Envelope diameter envelope_diameter65.8
Shell Rg shell_rg24.32
Envelope Rg envelope_rg18.65
Shape Rg shape_rg18.21
Total Rg total_rg19.34
Total atoms total_atoms1838
Residues n_residues229
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 dmax64.0
Rg (real space) rg_real19.28
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real8.3570e+06
I(0) uncertainty (real space) i0_real_error1.0600e+05
Rg (reciprocal space) rg_reciprocal19.27
I(0) (reciprocal space) i0_reciprocal8357000.0000
Solution quality estimate total_estimate0.8014
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1750000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4x31a_
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_id4x31A00
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)