3hao

Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles

Method: X-RAY DIFFRACTION Dmax: 82.4 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:L94A RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop, bicelle method;pH 3.7;310 K;350ul 4M NaPi, 2.5ul 6M 1.6-hexanediol, 17.5ul 100% triethylene glycol, 130ul H2O, pH 3.7, hanging drop, bicelle method, temperature 310K Resolution 2.49 Å R-free 0.245
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 14–262 Mutation:L94A RET RETINAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop, bicelle method;pH 3.7;310 K;350ul 4M NaPi, 2.5ul 6M 1.6-hexanediol, 17.5ul 100% triethylene glycol, 130ul H2O, pH 3.7, hanging drop, bicelle method, temperature 310K Resolution 2.49 Å R-free 0.245

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 200 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 Author chain B; 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 3hao

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3hao
Deposition date deposition_date2009-05-02
Structure title titleCrystal structure of bacteriorhodopsin mutant L94A 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_guinier24.59
Radius of gyration Rg (electron density) rg_electron23.49
Forward intensity I(0) i031001200.00
Molecular weight molecular_weight49912.0 kDa
Excluded volume excluded_volume65301 ų
Envelope volume envelope_volume72477 ų
Hydration-shell volume shell_volume25584 ų
Envelope diameter envelope_diameter85.4
Shell Rg shell_rg30.61
Envelope Rg envelope_rg23.67
Shape Rg shape_rg23.45
Total Rg total_rg24.54
Total atoms total_atoms3532
Residues n_residues452
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 dmax82.4
Rg (real space) rg_real24.54
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real3.1000e+07
I(0) uncertainty (real space) i0_real_error4.2280e+05
Rg (reciprocal space) rg_reciprocal24.55
I(0) (reciprocal space) i0_reciprocal31000000.0000
Solution quality estimate total_estimate0.8093
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.274
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5841000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3haoa_
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
Domain ID domain_idd3haob_
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 (2 domains)

Domain ID domain_id3haoA00
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
Domain ID domain_id3haoB00
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)