3nya

Crystal structure of the human beta2 adrenergic receptor in complex with the neutral antagonist alprenolol

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Beta-2 adrenergic receptor, Lysozyme

Enterobacteria phage T4

UniProt P00720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–161 Fragment:Chimeric protein of Beta-2 Adrenoreceptor 1-230, Lysozyme 2-161, Beta-2 adrenergic receptor 263-348 Mutation:E122W, N187E, C1054T, C1097A CLR CHOLESTEROL × 2 JTZ (2S)-1-[(1-methylethyl)amino]-3-(2-prop-2-en-1-ylphenoxy)propan-2-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:293 K;100 mM Bis-Tris Propane pH 6.6-6.8, 120 mM Na-tartrate, 3% 1,3 butanediol, 25-30% PEG 400, Lipidic Cubic Phase (LCP) Crystallization, temperature 293-295K Resolution 3.16 Å R-free 0.290

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.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 239–398; UniProt 2–161

Beta-2 adrenergic receptor, Lysozyme

Enterobacteria phage T4

UniProt P07550

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–230 Chain A; UniProt 263–348 Fragment:Chimeric protein of Beta-2 Adrenoreceptor 1-230, Lysozyme 2-161, Beta-2 adrenergic receptor 263-348 Mutation:E122W, N187E, C1054T, C1097A CLR CHOLESTEROL × 2 JTZ (2S)-1-[(1-methylethyl)amino]-3-(2-prop-2-en-1-ylphenoxy)propan-2-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:293 K;100 mM Bis-Tris Propane pH 6.6-6.8, 120 mM Na-tartrate, 3% 1,3 butanediol, 25-30% PEG 400, Lipidic Cubic Phase (LCP) Crystallization, temperature 293-295K Resolution 3.16 Å R-free 0.290

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.

143 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADRB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–238; UniProt 1–230 Author chain A; PDBConstruct 399–484; UniProt 263–348

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 3nya

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3nya
Deposition date deposition_date2010-07-14
Structure title titleCrystal structure of the human beta2 adrenergic receptor in complex with the neutral antagonist alprenolol
Keywords keywords;G Protein-coupled receptor, Lysozyme, Fusion, Transducer, Adrenergic, G-Proteins, Arrestins, Adrenaline, Alprenolol, Glycosylation, Palmitoylation, Phosphorylation, Membrane Protein, HYDROLASE, Structural Genomics, PSI-Biology, GPCR Network, GPCR ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.65
Radius of gyration Rg (electron density) rg_electron28.73
Forward intensity I(0) i036272700.00
Molecular weight molecular_weight51095.0 kDa
Excluded volume excluded_volume65830 ų
Envelope volume envelope_volume82627 ų
Hydration-shell volume shell_volume25618 ų
Envelope diameter envelope_diameter97.8
Shell Rg shell_rg33.89
Envelope Rg envelope_rg28.80
Shape Rg shape_rg28.71
Total Rg total_rg29.39
Total atoms total_atoms3601
Residues n_residues439
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 dmax98.0
Rg (real space) rg_real29.89
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real3.6270e+07
I(0) uncertainty (real space) i0_real_error5.1560e+05
Rg (reciprocal space) rg_reciprocal29.79
I(0) (reciprocal space) i0_reciprocal36270000.0000
Solution quality estimate total_estimate0.6296
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7223000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 0.050; Positv: 1.000; Valcen: 0.721; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3nyaA01
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_id3nyaA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)