1p8i

F219L BACTERIORHODOPSIN MUTANT

Method: X-RAY DIFFRACTION Dmax: 64.1 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 Mutation:F219L RET RETINAL × 3 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 X-RAY DIFFRACTION X-ray crystallization conditions:CUBIC LIPID PHASE;pH 5.6;295 K;MONO-OLEIN, POTASSIUM PHOSPHATE, pH 5.60, CUBIC LIPID PHASE, temperature 295K Resolution 1.86 Å R-free 0.220

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 1–249; 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 1p8i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p8i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p8i
Deposition date deposition_date2003-05-07
Structure title titleF219L BACTERIORHODOPSIN MUTANT
Keywords keywords;ION PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN, LIPIDS, PHOTORECEPTOR, HALOARCHAEA, 7-TRANSMEMBRANE, SERPENTINE, MEROHEDRAL TWINNING, PROTON TRANSPORT ;; PROTON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.32
Radius of gyration Rg (electron density) rg_electron18.54
Forward intensity I(0) i07486320.00
Molecular weight molecular_weight28867.0 kDa
Excluded volume excluded_volume40050 ų
Envelope volume envelope_volume44253 ų
Hydration-shell volume shell_volume19666 ų
Envelope diameter envelope_diameter64.5
Shell Rg shell_rg25.11
Envelope Rg envelope_rg19.07
Shape Rg shape_rg18.51
Total Rg total_rg20.06
Total atoms total_atoms2045
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 dmax64.1
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real7.4860e+06
I(0) uncertainty (real space) i0_real_error9.4720e+04
Rg (reciprocal space) rg_reciprocal19.36
I(0) (reciprocal space) i0_reciprocal7486000.0000
Solution quality estimate total_estimate0.7987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1578000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; 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_idd1p8ia_
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_id1p8iA00
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)