7z0a

Crystal structure of the ground state of bacteriorhodopsin at 1.22 Angstrom resolution

Method: X-RAY DIFFRACTION Dmax: 68.6 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 14–261 Non-standard monomer:Yes (specific site not provided by mmCIF) LFA EICOSANE × 24 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 OLA OLEIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;Na2HPO4 (5%) and KH2PO4 (95%) Resolution 1.22 Å R-free 0.167

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 7z0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z0a
Deposition date deposition_date2022-02-22
Structure title titleCrystal structure of the ground state of bacteriorhodopsin at 1.22 Angstrom resolution
Keywords keywordsrhodopsin, retinal, microbial rhodopsin, ion transport, proton pump, photocycle, ultrahigh resolution, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.52
Radius of gyration Rg (electron density) rg_electron18.43
Forward intensity I(0) i08033400.00
Molecular weight molecular_weight28864.0 kDa
Excluded volume excluded_volume39623 ų
Envelope volume envelope_volume42676 ų
Hydration-shell volume shell_volume19194 ų
Envelope diameter envelope_diameter70.6
Shell Rg shell_rg25.09
Envelope Rg envelope_rg18.98
Shape Rg shape_rg18.41
Total Rg total_rg19.83
Total atoms total_atoms4235
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 dmax68.6
Rg (real space) rg_real19.59
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real8.0330e+06
I(0) uncertainty (real space) i0_real_error1.0900e+05
Rg (reciprocal space) rg_reciprocal19.58
I(0) (reciprocal space) i0_reciprocal8033000.0000
Solution quality estimate total_estimate0.7678
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1800000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.721; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.816; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)