3p0g

Structure of a nanobody-stabilized active state of the beta2 adrenoceptor

Method: X-RAY DIFFRACTION Dmax: 104.0 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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–161 Fragment:UNP P07550 residues 1-230, 263-365, UNP P00720 residues 2-161 Mutation:N187E Camelid Antibody Fragment × 1 P0G 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;293 K;36-44% PEG 400, 100 mM Tris pH 8.0, 4% DMSO, 1% 1,2,3-heptanetriol, twin-syringe mixing method, temperature 293K Resolution 3.50 Å R-free 0.308

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–230 Chain A; UniProt 263–365 Fragment:UNP P07550 residues 1-230, 263-365, UNP P00720 residues 2-161 Mutation:N187E Camelid Antibody Fragment × 1 P0G 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;293 K;36-44% PEG 400, 100 mM Tris pH 8.0, 4% DMSO, 1% 1,2,3-heptanetriol, twin-syringe mixing method, temperature 293K Resolution 3.50 Å R-free 0.308

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 399–501; UniProt 263–365

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 3p0g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3p0g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3p0g
Deposition date deposition_date2010-09-28
Structure title titleStructure of a nanobody-stabilized active state of the beta2 adrenoceptor
Keywords keywordsBETA-2 ADRENOCEPTOR, agonist, nanobody, 7TM, GPCR, membrane, SIGNALING PROTEIN, Hydrolase, membrane protein; SIGNALING PROTEIN, Hydrolase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.01
Radius of gyration Rg (electron density) rg_electron27.24
Forward intensity I(0) i031829800.00
Molecular weight molecular_weight45962.0 kDa
Excluded volume excluded_volume58520 ų
Envelope volume envelope_volume71401 ų
Hydration-shell volume shell_volume24146 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg31.59
Envelope Rg envelope_rg27.64
Shape Rg shape_rg27.24
Total Rg total_rg27.76
Total atoms total_atoms3238
Residues n_residues405
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 dmax104.0
Rg (real space) rg_real29.93
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real3.2130e+07
I(0) uncertainty (real space) i0_real_error4.3990e+05
Rg (reciprocal space) rg_reciprocal28.32
I(0) (reciprocal space) i0_reciprocal31830000.0000
Solution quality estimate total_estimate0.5702
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.667
Kurtosis Kurtosis kurtosis-0.145
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha3.7530
Highest regularization parameter α highest_alpha5922000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.605; Stabil: 0.872; Sysdev: 0.000; Positv: 1.000; Valcen: 0.442; Smooth: 0.581

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3p0gA00
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_id3p0gB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)