1brr

X-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX

Method: X-RAY DIFFRACTION Dmax: 81.9 Å Quality: GOOD

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

PROTEIN (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 Other combination Homooligomer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–260 Chain B; UniProt 14–260 Chain C; UniProt 14–260 Non-standard monomer:Yes (specific site not provided by mmCIF) 3-O-sulfo-beta-D-galactopyranose-(1-6)-alpha-D-mannopyranose-(1-2)-alpha-D-glucopyranose × 2 RET RETINAL × 3 ARC 3,7,11,15-TETRAMETHYL-HEXADECAN-1-OL × 10 GOL GLYCEROL × 3 BGC beta-D-glucopyranose × 1 OCT N-OCTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.2;SEE REFERENCE 2, pH 5.2 Resolution 2.90 Å R-free 0.299

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_HALHA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–247; UniProt 14–260 Author chain B; PDBConstruct 1–247; UniProt 14–260 Author chain C; PDBConstruct 1–247; UniProt 14–260

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 1brr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1brr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1brr
Deposition date deposition_date1998-07-28
Structure title titleX-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX
Keywords keywordsPROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, LIPIDS, PHOTORECEPTOR, HALOARCHAEA, 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_guinier26.37
Radius of gyration Rg (electron density) rg_electron24.65
Forward intensity I(0) i071133100.00
Molecular weight molecular_weight80285.0 kDa
Excluded volume excluded_volume106470 ų
Envelope volume envelope_volume116910 ų
Hydration-shell volume shell_volume37335 ų
Envelope diameter envelope_diameter75.1
Shell Rg shell_rg33.65
Envelope Rg envelope_rg24.62
Shape Rg shape_rg24.65
Total Rg total_rg25.70
Total atoms total_atoms5672
Residues n_residues692
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 dmax81.9
Rg (real space) rg_real26.10
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real7.1130e+07
I(0) uncertainty (real space) i0_real_error1.0020e+06
Rg (reciprocal space) rg_reciprocal26.19
I(0) (reciprocal space) i0_reciprocal71140000.0000
Solution quality estimate total_estimate0.7923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.2
Skewness Skewness skewness-0.092
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28650000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1brra_
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
Domain ID domain_idd1brrb_
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
Domain ID domain_idd1brrc_
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 (3 domains)

Domain ID domain_id1brrA00
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
Domain ID domain_id1brrB00
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
Domain ID domain_id1brrC00
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 (2)

9. Files and Curves (10)