3mbv

Structure of bacterirhodopsin crystallized in betta-XylOC(16+4) meso phase

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 14–261 Fragment:UNP residues 14-261 RET RETINAL × 3 BXC (3R,7R,11R)-3,7,11,15-tetramethylhexadecyl alpha-D-ribopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:in meso crystallization;298 K;in meso crystallization, temperature 298K Resolution 2.00 Å R-free 0.203

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 1–248; UniProt 14–261

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 3mbv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mbv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mbv
Deposition date deposition_date2010-03-26
Structure title titleStructure of bacterirhodopsin crystallized in betta-XylOC(16+4) meso phase
Keywords keywordsmembrane protein; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.88
Radius of gyration Rg (electron density) rg_electron17.79
Forward intensity I(0) i08150050.00
Molecular weight molecular_weight24997.0 kDa
Excluded volume excluded_volume32930 ų
Envelope volume envelope_volume35270 ų
Hydration-shell volume shell_volume16830 ų
Envelope diameter envelope_diameter61.7
Shell Rg shell_rg23.77
Envelope Rg envelope_rg18.17
Shape Rg shape_rg17.78
Total Rg total_rg18.88
Total atoms total_atoms1769
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 dmax61.3
Rg (real space) rg_real18.90
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real8.1500e+06
I(0) uncertainty (real space) i0_real_error1.1480e+05
Rg (reciprocal space) rg_reciprocal18.90
I(0) (reciprocal space) i0_reciprocal8150000.0000
Solution quality estimate total_estimate0.8112
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1807000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; 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 (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3mbva_
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_id3mbvA00
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)