3haq

Crystal structure of bacteriorhodopsin mutant I148A crystallized from bicelles

Method: X-RAY DIFFRACTION Dmax: 62.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 14–262 Mutation:I148A RET RETINAL × 1 HP6 HEPTANE × 1 DD9 nonane × 3 D12 DODECANE × 2 D10 DECANE × 1 R16 HEXADECANE × 1 CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop, bicelle method;pH 3.9;310 K;2.2 M sodium phosphate, 180 mM 1,6-hexanediol, 3.5 % triethylene glycol, PFPC used as cryoprotectant, pH 3.9, hanging drop, bicelle method, temperature 310K Resolution 2.30 Å R-free 0.236

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 3haq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3haq
Deposition date deposition_date2009-05-02
Structure title titleCrystal structure of bacteriorhodopsin mutant I148A crystallized from bicelles
Keywords keywords;bacteriorhodopsin, packing force, van der Waals, evolutionary constraint, membrane protein, integral membrane protein, helical membrane protein, proton transport, Cell membrane, Chromophore, Hydrogen ion transport, Ion transport, Membrane, Photoreceptor protein, Pyrrolidone carboxylic acid, Receptor, Retinal protein, Sensory transduction, Transmembrane, Transport, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.94
Radius of gyration Rg (electron density) rg_electron18.23
Forward intensity I(0) i08140480.00
Molecular weight molecular_weight26510.0 kDa
Excluded volume excluded_volume35579 ų
Envelope volume envelope_volume38831 ų
Hydration-shell volume shell_volume17834 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg24.47
Envelope Rg envelope_rg18.72
Shape Rg shape_rg18.20
Total Rg total_rg19.52
Total atoms total_atoms1876
Residues n_residues226
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 dmax62.0
Rg (real space) rg_real18.96
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real8.1400e+06
I(0) uncertainty (real space) i0_real_error1.2010e+05
Rg (reciprocal space) rg_reciprocal18.96
I(0) (reciprocal space) i0_reciprocal8140000.0000
Solution quality estimate total_estimate0.8108
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.374
Kurtosis Kurtosis kurtosis-0.351
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1701000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3haqa_
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_id3haqA00
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)