2rh1

High resolution crystal structure of human B2-adrenergic G protein-coupled receptor.

Method: X-RAY DIFFRACTION Dmax: 98.5 Å Quality: REASONABLE

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

beta-2-adrenergic receptor/T4-lysozyme chimera

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 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–161 Mutation:N187E, C54T, C97A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 6 CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 2 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC MESOPHASE;pH 6.75;293 K;30-35% v/v PEG 400, 0.1-0.2 M Na2SO4, 0.1 M Bis-tris propane pH 6.5-7.0, 5-7% 1,4-Butanediol, 8-10% Cholesterol, 52-50% Monoolein, pH 6.75, LIPIDIC MESOPHASE, temperature 293K Resolution 2.40 Å R-free 0.232

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 238–397; UniProt 2–161

beta-2-adrenergic receptor/T4-lysozyme chimera

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 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–230 Chain A; UniProt 263–365 Mutation:N187E, C54T, C97A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 6 CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 BU1 1,4-BUTANEDIOL × 2 ACM ACETAMIDE × 1 CLR CHOLESTEROL × 3 PLM PALMITIC ACID × 1 12P DODECAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC MESOPHASE;pH 6.75;293 K;30-35% v/v PEG 400, 0.1-0.2 M Na2SO4, 0.1 M Bis-tris propane pH 6.5-7.0, 5-7% 1,4-Butanediol, 8-10% Cholesterol, 52-50% Monoolein, pH 6.75, LIPIDIC MESOPHASE, temperature 293K Resolution 2.40 Å R-free 0.232

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 8–237; UniProt 1–230 Author chain A; PDBConstruct 398–500; 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 2rh1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rh1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rh1
Deposition date deposition_date2007-10-05
Structure title titleHigh resolution crystal structure of human B2-adrenergic G protein-coupled receptor.
Keywords keywords;GPCR, 7TM, adrenergic, fusion, lipidic cubic phase, lipidic, mesophase, cholesterol, membrane protein, MEMBRANE PROTEIN - HYDROLASE COMPLEX, Structural Genomics, PSI-2, Protein Structure Initiative, Accelerated Technologies Center for Gene to 3D Structure, ATCG3D, GPCR Network ;; MEMBRANE PROTEIN / HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.81
Radius of gyration Rg (electron density) rg_electron29.05
Forward intensity I(0) i039759400.00
Molecular weight molecular_weight53477.0 kDa
Excluded volume excluded_volume68787 ų
Envelope volume envelope_volume84064 ų
Hydration-shell volume shell_volume25672 ų
Envelope diameter envelope_diameter99.2
Shell Rg shell_rg34.30
Envelope Rg envelope_rg29.13
Shape Rg shape_rg29.04
Total Rg total_rg29.63
Total atoms total_atoms3756
Residues n_residues442
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 dmax98.5
Rg (real space) rg_real30.05
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real3.9760e+07
I(0) uncertainty (real space) i0_real_error6.4930e+05
Rg (reciprocal space) rg_reciprocal29.96
I(0) (reciprocal space) i0_reciprocal39760000.0000
Solution quality estimate total_estimate0.6298
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8110000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 0.050; Positv: 1.000; Valcen: 0.712; Smooth: 0.900

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2rh1a1
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.13.1.3 — Amine receptor-like
Domain ID domain_idd2rh1a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.3 — Phage lysozyme

CATH v4.4 (2 domains)

Domain ID domain_id2rh1A01
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_id2rh1A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (2)

9. Files and Curves (10)