1fbk

CRYSTAL STRUCTURE OF CYTOPLASMICALLY OPEN CONFORMATION OF BACTERIORHODOPSIN

Method: ELECTRON CRYSTALLOGRAPHY Dmax: 62.1 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 Mutation:D96G,F171C,F219L RET RETINAL × 3 ELECTRON CRYSTALLOGRAPHY X-ray crystallization conditions:naturally occurring in vivo;pH 7;310 K;crystals are increased in size by fusion and annealing using detergents, pH 7, naturally occurring in vivo, temperature 37K Resolution 3.20 Å R-free 0.321

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 1–248; 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 1fbk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fbk
Deposition date deposition_date2000-07-15
Structure title titleCRYSTAL STRUCTURE OF CYTOPLASMICALLY OPEN CONFORMATION OF BACTERIORHODOPSIN
Keywords keywordsPROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, TWO-DIMENSIONAL CRYSTAL ELECTRON DIFFRACTION, SINGLE CRYSTAL, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON CRYSTALLOGRAPHY

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

Radius of gyration Rg (Guinier) rg_guinier19.06
Radius of gyration Rg (electron density) rg_electron17.91
Forward intensity I(0) i08500900.00
Molecular weight molecular_weight24716.0 kDa
Excluded volume excluded_volume32301 ų
Envelope volume envelope_volume35456 ų
Hydration-shell volume shell_volume16812 ų
Envelope diameter envelope_diameter62.9
Shell Rg shell_rg23.72
Envelope Rg envelope_rg18.33
Shape Rg shape_rg17.89
Total Rg total_rg18.99
Total atoms total_atoms1746
Residues n_residues225
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 dmax62.1
Rg (real space) rg_real19.06
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real8.5010e+06
I(0) uncertainty (real space) i0_real_error1.1310e+05
Rg (reciprocal space) rg_reciprocal19.06
I(0) (reciprocal space) i0_reciprocal8501000.0000
Solution quality estimate total_estimate0.8133
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1652000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fbka_
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_id1fbkA00
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)