5br2

Structure of bacteriorhodopsin crystallized from ND-MSP1

Method: X-RAY DIFFRACTION Dmax: 58.9 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 14–262 Not recorded RET RETINAL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;The crystals were grown using the in meso crystallization method Resolution 1.80 Å R-free 0.237

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 5br2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5br2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5br2
Deposition date deposition_date2015-05-29
Structure title titleStructure of bacteriorhodopsin crystallized from ND-MSP1
Keywords keywordsMembrane protein, Proton pump, 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_guinier18.38
Radius of gyration Rg (electron density) rg_electron17.35
Forward intensity I(0) i07442610.00
Molecular weight molecular_weight23611.0 kDa
Excluded volume excluded_volume31014 ų
Envelope volume envelope_volume32909 ų
Hydration-shell volume shell_volume16134 ų
Envelope diameter envelope_diameter59.9
Shell Rg shell_rg23.25
Envelope Rg envelope_rg17.75
Shape Rg shape_rg17.35
Total Rg total_rg18.41
Total atoms total_atoms1673
Residues n_residues216
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 dmax58.9
Rg (real space) rg_real18.37
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real7.4430e+06
I(0) uncertainty (real space) i0_real_error8.9230e+04
Rg (reciprocal space) rg_reciprocal18.38
I(0) (reciprocal space) i0_reciprocal7443000.0000
Solution quality estimate total_estimate0.8135
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1511000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; 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_idd5br2a_
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_id5br2A00
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)