1m0l

BACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 63.3 Å Quality: GOOD

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

BACTERIORHODOPSIN

Halobacterium salinarum

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 1–262 Not recorded LI1 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL × 39 SQU 2,10,23-TRIMETHYL-TETRACOSANE × 3 RET RETINAL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:CUBIC LIPID PHASE;pH 5.6;295 K;CUBIC LIPID PHASE WITH MONO-OLEIN, PRECIPITANT PHOSPHATE, pH 5.60, temperature 295K Resolution 1.47 Å R-free 0.179

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_HALN1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–262; UniProt 1–262

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 1m0l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m0l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m0l
Deposition date deposition_date2002-06-13
Structure title titleBACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION
Keywords keywords;ION PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, LIPIDS, PHOTORECEPTOR, HALOARCHAEA, 7-TRANSMEMBRANE, SERPENTINE, MEROHEDRAL TWINNING, ION TRANSPORT ;; ION TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.15
Radius of gyration Rg (electron density) rg_electron18.44
Forward intensity I(0) i07455400.00
Molecular weight molecular_weight28931.0 kDa
Excluded volume excluded_volume40154 ų
Envelope volume envelope_volume43569 ų
Hydration-shell volume shell_volume19497 ų
Envelope diameter envelope_diameter63.4
Shell Rg shell_rg25.01
Envelope Rg envelope_rg18.92
Shape Rg shape_rg18.40
Total Rg total_rg19.97
Total atoms total_atoms2050
Residues n_residues222
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 dmax63.3
Rg (real space) rg_real19.19
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real7.4550e+06
I(0) uncertainty (real space) i0_real_error9.8890e+04
Rg (reciprocal space) rg_reciprocal19.19
I(0) (reciprocal space) i0_reciprocal7455000.0000
Solution quality estimate total_estimate0.8030
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1516000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1m0la_
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_id1m0lA00
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)