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2y03

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE

Method: X-RAY DIFFRACTION Dmax: 95.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BETA-1 ADRENERGIC RECEPTOR

MELEAGRIS GALLOPAVO

UniProt P07700

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 33–368 Fragment：RESIDUES 33-368 Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 1 2CV HEGA-10 × 3 5FW ISOPRENALINE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R)-ISOPRENALINE, 0.45MG/ML CHS, 0.5% HEGA-10, 0.1M TRIS-HCL PH8.5, 28% PEG600 AT 4 DEGREES C Resolution 2.85 Å R-free 0.254
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 33–368 Fragment：RESIDUES 33-368 Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 1 2CV HEGA-10 × 3 5FW ISOPRENALINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R)-ISOPRENALINE, 0.45MG/ML CHS, 0.5% HEGA-10, 0.1M TRIS-HCL PH8.5, 28% PEG600 AT 4 DEGREES C Resolution 2.85 Å R-free 0.254
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 33–368 Chain B； UniProt 33–368 Fragment：RESIDUES 33-368 Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 6 5FW ISOPRENALINE × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R)-ISOPRENALINE, 0.45MG/ML CHS, 0.5% HEGA-10, 0.1M TRIS-HCL PH8.5, 28% PEG600 AT 4 DEGREES C Resolution 2.85 Å R-free 0.254

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.

Other PDB Difference from Current Entry 2Y03 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DEP MEMBRANE PROTEIN, NMR, 1 STRUCTURE Deposited 1995-08-23 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 345–359（15 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 2 NA SODIUM ION × 2 SOG octyl 1-thio-beta-D-glucopyranoside × 6 D10 DECANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain C 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain C 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain D 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain D 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain D 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 2 NA SODIUM ION × 2 SOG octyl 1-thio-beta-D-glucopyranoside × 6 D10 DECANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 NA SODIUM ION × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 D10 DECANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 NA SODIUM ION × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain C 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain C 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 NA SODIUM ION × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 D10 DECANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2VT4 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL Deposited 2008-05-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain D 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain D 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 NA SODIUM ION × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.1；VAPOUR DIFFUSION. EQUAL VOLUMES OF PROTEIN (6MG/ML) IN 10MM TRIS-HCL PH7.7, 50MM NACL, 0.1MM EDTA, 0.35% OCTYLTHIOGLUCOSIDE, 0.5MM CYANOPINDOLOL AND RESERVOIR 0.1M ADA, PH 6.9-7.3, 29-32% PEG600.
Resolution 2.70 Å R-free 0.268
2Y00 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB92) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 Y00 DOBUTAMINE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (14.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 1.3MG/ML CHS, 0.55% HEGA-10, 0.1M TRIS-HCL PH8.5, 25% PEG600 AT 4 DEGREES C
Resolution 2.50 Å R-free 0.256
2Y00 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB92) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 Y00 DOBUTAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (14.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 1.3MG/ML CHS, 0.55% HEGA-10, 0.1M TRIS-HCL PH8.5, 25% PEG600 AT 4 DEGREES C
Resolution 2.50 Å R-free 0.256
2Y00 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB92) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 4 2CV HEGA-10 × 10 Y00 DOBUTAMINE × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (14.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 1.3MG/ML CHS, 0.55% HEGA-10, 0.1M TRIS-HCL PH8.5, 25% PEG600 AT 4 DEGREES C
Resolution 2.50 Å R-free 0.256
2Y01 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB102) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 Y00 DOBUTAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 0.9MG/ML CHS, 0.6% HEGA-10, 0.1M BICINE PH9, 25% PEG600 AT 4 DEGREES C, pH 9.0
Resolution 2.60 Å R-free 0.266
2Y01 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB102) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 Y00 DOBUTAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 0.9MG/ML CHS, 0.6% HEGA-10, 0.1M BICINE PH9, 25% PEG600 AT 4 DEGREES C, pH 9.0
Resolution 2.60 Å R-free 0.266
2Y01 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB102) Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 4 2CV HEGA-10 × 10 Y00 DOBUTAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (15MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-DOBUTAMINE, 0.9MG/ML CHS, 0.6% HEGA-10, 0.1M BICINE PH9, 25% PEG600 AT 4 DEGREES C, pH 9.0
Resolution 2.60 Å R-free 0.266
2Y02 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 WHJ CARMOTEROL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, R)-CARMOTEROL, 1.9MG/ML CHS, 0.65% HEGA-10, 0.1M BICINE PH9.0, 26% PEG600 AT 4 DEGREES C
Resolution 2.60 Å R-free 0.268
2Y02 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 WHJ CARMOTEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, R)-CARMOTEROL, 1.9MG/ML CHS, 0.65% HEGA-10, 0.1M BICINE PH9.0, 26% PEG600 AT 4 DEGREES C
Resolution 2.60 Å R-free 0.268
2Y02 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 4 2CV HEGA-10 × 10 WHJ CARMOTEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, R)-CARMOTEROL, 1.9MG/ML CHS, 0.65% HEGA-10, 0.1M BICINE PH9.0, 26% PEG600 AT 4 DEGREES C
Resolution 2.60 Å R-free 0.268
2Y04 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST SALBUTAMOL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 68H SALBUTAMOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-SALBUTAMOL, 1.0MG/ML CHS, 0.5% HEGA-10, 0.1M BICINE PH9.0, 28% PEG400 AT 4 DEGREES C
Resolution 3.05 Å R-free 0.255
2Y04 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST SALBUTAMOL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 68H SALBUTAMOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-SALBUTAMOL, 1.0MG/ML CHS, 0.5% HEGA-10, 0.1M BICINE PH9.0, 28% PEG400 AT 4 DEGREES C
Resolution 3.05 Å R-free 0.255
2Y04 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST SALBUTAMOL Deposited 2010-11-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-368
Chain B 33–368（336 aa） Fragment：RESIDUES 33-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 4 2CV HEGA-10 × 10 68H SALBUTAMOL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；SITTING DROP VAPOUR DIFFUSION, PROTEIN (16.5MG/ML) IN 100MM NACL, 0.1MM EDTA, 1.0MM (R, S)-SALBUTAMOL, 1.0MG/ML CHS, 0.5% HEGA-10, 0.1M BICINE PH9.0, 28% PEG400 AT 4 DEGREES C
Resolution 3.05 Å R-free 0.255
2YCW TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 2CV HEGA-10 × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；pH 8.1
Resolution 3.00 Å R-free 0.295
2YCW TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES CAU (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol × 1 2CV HEGA-10 × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.1；pH 8.1
Resolution 3.00 Å R-free 0.295
2YCX TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CYANOPINDOLOL Deposited 2011-03-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–367（335 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES P32 Cyanopindolol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.3；pH 7.3
Resolution 3.25 Å R-free 0.325
2YCX TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CYANOPINDOLOL Deposited 2011-03-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–367（335 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES P32 Cyanopindolol × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.3；pH 7.3
Resolution 3.25 Å R-free 0.325
2YCY TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CYANOPINDOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；pH 7.2
Resolution 3.15 Å R-free 0.292
2YCY TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CYANOPINDOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES P32 Cyanopindolol × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；pH 7.2
Resolution 3.15 Å R-free 0.292
2YCZ TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST IODOCYANOPINDOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain A 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES I32 4-{[(2S)-3-(tert-butylamino)-2-hydroxypropyl]oxy}-3-iodo-1H-indole-2-carbonitrile × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 3.65 Å R-free 0.270
2YCZ TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST IODOCYANOPINDOLOL Deposited 2011-03-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 272–276（5 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 279–367（89 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：YES Mutation：YES Mutation：YES I32 4-{[(2S)-3-(tert-butylamino)-2-hydroxypropyl]oxy}-3-iodo-1H-indole-2-carbonitrile × 1 SOG octyl 1-thio-beta-D-glucopyranoside × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 3.65 Å R-free 0.270
3ZPQ Thermostabilised turkey beta1 adrenergic receptor with 4-(piperazin-1- yl)-1H-indole bound (compound 19) Deposited 2013-03-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain A 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 4 XF5 4-(PIPERAZIN-1-YL)-1H-INDOLE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1M BICINE PH9.0, 24% PEG600, 4C
Resolution 2.80 Å R-free 0.274
3ZPQ Thermostabilised turkey beta1 adrenergic receptor with 4-(piperazin-1- yl)-1H-indole bound (compound 19) Deposited 2013-03-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain B 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES Y01 CHOLESTEROL HEMISUCCINATE × 2 2CV HEGA-10 × 5 XF5 4-(PIPERAZIN-1-YL)-1H-INDOLE × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1M BICINE PH9.0, 24% PEG600, 4C
Resolution 2.80 Å R-free 0.274
3ZPR Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline bound Deposited 2013-03-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain A 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES NA SODIUM ION × 2 Y01 CHOLESTEROL HEMISUCCINATE × 2 3WC 4-METHYL-2-(PIPERAZIN-1-YL) QUINOLINE × 1 2CV HEGA-10 × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1M BICINE PH9.0, 24% PEG600, 4C
Resolution 2.70 Å R-free 0.266
3ZPR Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline bound Deposited 2013-03-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain B 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES NA SODIUM ION × 2 Y01 CHOLESTEROL HEMISUCCINATE × 2 3WC 4-METHYL-2-(PIPERAZIN-1-YL) QUINOLINE × 1 2CV HEGA-10 × 5 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1M BICINE PH9.0, 24% PEG600, 4C
Resolution 2.70 Å R-free 0.266
4AMI Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist bucindolol Deposited 2012-03-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain A 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES G90 2-[(2S)-3-[[1-(1H-indol-3-yl)-2-methyl-propan-2-yl]amino]-2-oxidanyl-propoxy]benzenecarbonitrile × 1 2CV HEGA-10 × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1 M BICINE PH 9.0, 22% PEG 600, 4 DEGREES CELSIUS.
Resolution 3.20 Å R-free 0.279
4AMI Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist bucindolol Deposited 2012-03-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain B 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES G90 2-[(2S)-3-[[1-(1H-indol-3-yl)-2-methyl-propan-2-yl]amino]-2-oxidanyl-propoxy]benzenecarbonitrile × 1 2CV HEGA-10 × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1 M BICINE PH 9.0, 22% PEG 600, 4 DEGREES CELSIUS.
Resolution 3.20 Å R-free 0.279
4AMJ Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist carvedilol Deposited 2012-03-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain A 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES CVD (2S)-1-(8H-CARBAZOL-4-YLOXY)-3-[2-(2-METHOXYPHENOXY)ETHYLAMINO]PROPAN-2-OL × 1 NA SODIUM ION × 1 2CV HEGA-10 × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1 M BICINE PH 9.0, 22% PEG 600, 4 DEGREES CELSIUS.
Resolution 2.30 Å R-free 0.240
4AMJ Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist carvedilol Deposited 2012-03-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–243（211 aa） Fragment：RESIDUES 33-243,272-368
Chain B 272–368（97 aa） Fragment：RESIDUES 33-243,272-368
Mutation：YES Mutation：YES CVD (2S)-1-(8H-CARBAZOL-4-YLOXY)-3-[2-(2-METHOXYPHENOXY)ETHYLAMINO]PROPAN-2-OL × 1 NA SODIUM ION × 1 2CV HEGA-10 × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；277 K；0.1 M BICINE PH 9.0, 22% PEG 600, 4 DEGREES CELSIUS.
Resolution 2.30 Å R-free 0.240
4BVN Ultra-thermostable beta1-adrenoceptor with cyanopindolol bound Deposited 2013-06-26 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–243（211 aa）
Chain A 272–368（97 aa）
Mutation：YES Mutation：YES NA SODIUM ION × 2 P32 Cyanopindolol × 1 MHA (CARBAMOYLMETHYL-CARBOXYMETHYL-AMINO)-ACETIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 7 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 7；293 K；25% PEG 600, 0.1M ADA PH7.0 LIPID CUBIC PHASE (LCP) TEMPERATURE 293K
Resolution 2.10 Å R-free 0.246
4GPO Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor Deposited 2012-08-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 31–368（338 aa） Fragment：RESIDUES 33-243,272-276,279-367
Chain B 31–368（338 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：STABILISING MUTATIONS Mutation：STABILISING MUTATIONS No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；20mM sodium acetate, 100-300mM ammonium sulfate, 26~30% PEG200, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.50 Å R-free 0.355
5A8E thermostabilised beta1-adrenoceptor with rationally designed inverse agonist 7-methylcyanopindolol bound Deposited 2015-07-15 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa）
Mutation：YES NA SODIUM ION × 2 XTK 4-[(2S)-3-(tert-butylamino)-2-hydroxypropoxy]-7-methyl-1H-indole-2-carbonitrile × 1 MHA (CARBAMOYLMETHYL-CARBOXYMETHYL-AMINO)-ACETIC ACID × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 7；293 K；25% PEG600, 0.1M ADA PH7.0, LIPIDIC CUBIC PHASE (LCP), TEMPERATURE 293K
Resolution 2.40 Å R-free 0.248
5F8U Ligand occupancy in crystal structure of beta1-adrenergic receptor previously submitted by Huang et al Deposited 2015-12-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–368（336 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：R68S,M90V,Y227A,A282L,F327A,F338MC116L, C358A P32 Cyanopindolol × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.35 Å R-free 0.382
5F8U Ligand occupancy in crystal structure of beta1-adrenergic receptor previously submitted by Huang et al Deposited 2015-12-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–368（336 aa） Fragment：RESIDUES 33-243,272-276,279-367
Mutation：R68S,M90V,Y227A,A282L,F327A,F338MC116L, C358A P32 Cyanopindolol × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.35 Å R-free 0.382
6H7J ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST ISOPRENALINE AND NANOBODY Nb80 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 5FW ISOPRENALINE × 1 NA SODIUM ION × 1 2CV HEGA-10 × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.80 Å R-free 0.317
6H7J ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST ISOPRENALINE AND NANOBODY Nb80 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 5FW ISOPRENALINE × 1 NA SODIUM ION × 1 2CV HEGA-10 × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.80 Å R-free 0.317
6H7L ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST DOBUTAMINE AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 2CV HEGA-10 × 6 NA SODIUM ION × 1 Y00 DOBUTAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.70 Å R-free 0.278
6H7L ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST DOBUTAMINE AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 2CV HEGA-10 × 3 NA SODIUM ION × 1 Y00 DOBUTAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.70 Å R-free 0.278
6H7M ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST SALBUTAMOL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 2CV HEGA-10 × 3 68H SALBUTAMOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.76 Å R-free 0.285
6H7M ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST SALBUTAMOL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A 2CV HEGA-10 × 4 68H SALBUTAMOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.76 Å R-free 0.285
6H7N ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST XAMOTEROL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A FVK ~{N}-[2-[[(2~{S})-2-oxidanyl-3-(4-oxidanylphenoxy)propyl]amino]ethyl]morpholine-4-carboxamide × 1 NA SODIUM ION × 1 2CV HEGA-10 × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.50 Å R-free 0.266
6H7N ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND PARTIAL AGONIST XAMOTEROL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A FVK ~{N}-[2-[[(2~{S})-2-oxidanyl-3-(4-oxidanylphenoxy)propyl]amino]ethyl]morpholine-4-carboxamide × 1 NA SODIUM ION × 1 2CV HEGA-10 × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.50 Å R-free 0.266
6H7O ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND WEAK PARTIAL AGONIST CYANOPINDOLOL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A P32 Cyanopindolol × 1 NA SODIUM ION × 1 2CV HEGA-10 × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.80 Å R-free 0.274
6H7O ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND WEAK PARTIAL AGONIST CYANOPINDOLOL AND NANOBODY Nb6B9 Deposited 2018-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 44–368（325 aa）
Mutation：R68S,M90V,C116L,F327A,F338M,C358A P32 Cyanopindolol × 1 NA SODIUM ION × 1 2CV HEGA-10 × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.80 Å R-free 0.274
6IBL ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST FORMOTEROL AND NANOBODY Nb80 Deposited 2018-11-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 44–368（325 aa）
Mutation：C32S,C35S,C32S,C35S H98 ~{N}-[5-[(1~{R})-2-[[(2~{R})-1-(4-methoxyphenyl)propan-2-yl]amino]-1-oxidanyl-ethyl]-2-oxidanyl-phenyl]methanamide × 1 NA SODIUM ION × 1 2CV HEGA-10 × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.70 Å R-free 0.277
6IBL ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST FORMOTEROL AND NANOBODY Nb80 Deposited 2018-11-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 44–368（325 aa）
Mutation：C32S,C35S,C32S,C35S H98 ~{N}-[5-[(1~{R})-2-[[(2~{R})-1-(4-methoxyphenyl)propan-2-yl]amino]-1-oxidanyl-ethyl]-2-oxidanyl-phenyl]methanamide × 1 NA SODIUM ION × 1 2CV HEGA-10 × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes-NaOH pH7.5 and 21-24% PEG1500
Resolution 2.70 Å R-free 0.277
6TKO Phosphorylated turkey beta1 adrenoceptor with bound agonist formoterol coupled to arrestin-2 in lipid nanodisc. Deposited 2019-11-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 32–357（326 aa）
Mutation：S32G M44C M90V V103C C116L E130W D322K F327A F338M C358A Non-standard monomer：Yes (specific site not provided by mmCIF) H98 ~{N}-[5-[(1~{R})-2-[[(2~{R})-1-(4-methoxyphenyl)propan-2-yl]amino]-1-oxidanyl-ethyl]-2-oxidanyl-phenyl]methanamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 2-3 seconds before plunging. Liquid ethane maintained at 92.15 K.
Resolution 3.30 Å

25 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADRB1_MELGA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–310； UniProt 33–368 Author chain B； PDBConstruct 3–310； UniProt 33–368

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 2y03

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2y03
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2y03
Deposition date deposition_date2010-11-30
Structure title titleTURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE
Keywords keywords;RECEPTOR, G PROTEIN COUPLED RECEPTOR, SEVEN-HELIX RECEPTOR, INTEGRAL MEMBRANE PROTEIN, THERMOSTABILISING POINT MUTATIONS, GPCR, 7TM RECEPTOR ;; RECEPTOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.81 Å
Radius of gyration Rg (electron density) rg_electron27.33 Å
Forward intensity I(0) i062229400.00
Molecular weight molecular_weight69039.0 kDa
Excluded volume excluded_volume89704 ų
Envelope volume envelope_volume111190 ų
Hydration-shell volume shell_volume33564 ų
Envelope diameter envelope_diameter105.5 Å
Shell Rg shell_rg34.66 Å
Envelope Rg envelope_rg28.07 Å
Shape Rg shape_rg27.29 Å
Total Rg total_rg28.31 Å
Total atoms total_atoms4852
Residues n_residues586
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.3 Å
Rg (real space) rg_real28.73 Å
Rg uncertainty (real space) rg_real_error0.66 Å
I(0) (real space) i0_real6.2230e+07
I(0) uncertainty (real space) i0_real_error8.5720e+05
Rg (reciprocal space) rg_reciprocal28.77 Å
I(0) (reciprocal space) i0_reciprocal62230000.0000
Solution quality estimate total_estimate0.8953
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4 Å
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.2750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10960000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.995
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2y03a_
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_idd2y03b_
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

CATH v4.4 (2 domains)

Domain ID domain_id2y03A00
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_id2y03B00
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
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8. Citations (3)

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9. Files and Curves (10)