2vt4

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL

Method: X-RAY DIFFRACTION D_max: 124.6 Å Quality: GOOD

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

BETA1 ADRENERGIC RECEPTOR

MELEAGRIS GALLOPAVO

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 33–243 Chain A； UniProt 272–276 Chain A； UniProt 279–367 Chain B； UniProt 33–243 Chain B； UniProt 272–276 Chain B； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 33–243 Chain C； UniProt 272–276 Chain C； UniProt 279–367 Chain D； UniProt 33–243 Chain D； UniProt 272–276 Chain D； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 33–243 Chain A； UniProt 272–276 Chain A； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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
4	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 33–243 Chain B； UniProt 272–276 Chain B； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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
5	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 33–243 Chain C； UniProt 272–276 Chain C； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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
6	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain D； UniProt 33–243 Chain D； UniProt 272–276 Chain D； UniProt 279–367	Fragment：RESIDUES 33-243,272-276,279-367 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

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 2VT4	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
2Y00 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB92) Deposited 2010-11-30	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 33–368（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 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 33–368（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 construct Different mutation/modification 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 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 33–368（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 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 33–368（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 construct Different mutation/modification 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 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 33–368（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 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 33–368（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 construct Different mutation/modification 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
2Y03 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE Deposited 2010-11-30	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 33–368（336 aa） 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
2Y03 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE Deposited 2010-11-30	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 33–368（336 aa） 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
2Y03 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE Deposited 2010-11-30	Different construct Different mutation/modification 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 × 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
2Y04 TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST SALBUTAMOL Deposited 2010-11-30	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 33–368（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 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 33–368（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 construct Different mutation/modification 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 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 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 mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–367（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 mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 33–367（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 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 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 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 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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 33-243,272-368 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 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） 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 mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–368（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 50 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 3–213； UniProt 33–243 Author chain A； PDBConstruct 214–218； UniProt 272–276 Author chain A； PDBConstruct 219–307； UniProt 279–367 Author chain B； PDBConstruct 3–213； UniProt 33–243 Author chain B； PDBConstruct 214–218； UniProt 272–276 Author chain B； PDBConstruct 219–307； UniProt 279–367 Author chain C； PDBConstruct 3–213； UniProt 33–243 Author chain C； PDBConstruct 214–218； UniProt 272–276 Author chain C； PDBConstruct 219–307； UniProt 279–367 Author chain D； PDBConstruct 3–213； UniProt 33–243 Author chain D； PDBConstruct 214–218； UniProt 272–276 Author chain D； PDBConstruct 219–307； UniProt 279–367

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2vt4
Deposition date deposition_date	2008-05-09
Structure title title	TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL
Keywords keywords	;GPCR, MEMBRANE, RECEPTOR, PALMITATE, TRANSDUCER, ANTAGONIST BOUND FORM, INTEGRAL MEMBRANE PROTEIN, G-PROTEIN COUPLED RECEPTOR, G PROTEIN COUPLED RECEPTOR, THERMOSTABILISING POINT MUTATIONS, PHOSPHOPROTEIN, SEVEN-HELIX RECEPTOR, LIPOPROTEIN, 7TM RECEPTOR, GLYCOPROTEIN, TRANSMEMBRANE ;; RECEPTOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	37.71 Å
Radius of gyration Rg (electron density) rg_electron	37.13 Å
Forward intensity I(0) i0	196940000.00
Molecular weight molecular_weight	127410.0 kDa
Excluded volume excluded_volume	165310 Å³
Envelope volume envelope_volume	219840 Å³
Hydration-shell volume shell_volume	48825 Å³
Envelope diameter envelope_diameter	129.9 Å
Shell Rg shell_rg	43.65 Å
Envelope Rg envelope_rg	36.91 Å
Shape Rg shape_rg	37.11 Å
Total Rg total_rg	37.67 Å
Total atoms total_atoms	8945
Residues n_residues	1085
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	124.6 Å
Rg (real space) rg_real	37.71 Å
Rg uncertainty (real space) rg_real_error	1.12 Å
I(0) (real space) i0_real	1.9690e+08
I(0) uncertainty (real space) i0_real_error	3.9490e+06
Rg (reciprocal space) rg_reciprocal	37.71 Å
I(0) (reciprocal space) i0_reciprocal	196900000.0000
Solution quality estimate total_estimate	0.8952
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	44.5 Å
Skewness Skewness skewness	0.305
Kurtosis Kurtosis kurtosis	-0.450
Angular range angular_range	— – 0.2100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	20000000.0000
Real-space data points n_real_points	43
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.941

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	BETA1 ADRENERGIC RECEPTOR
Molecular weight formula_weight	35752.6 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8976

MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVVGLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLAFPRKADRRLHHHHHH

来源 Source

来源生物 organism	MELEAGRIS GALLOPAVO
通用名 common_name	COMMON TURKEY
NCBI Class编号 ncbi_taxonomy_id	9103
宿主生物 host_organism	TRICHOPLUSIA NI

Entity 2 Entity 2 non-polymer

Description description	Cyanopindolol
Molecular weight formula_weight	287.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	octyl 1-thio-beta-D-glucopyranoside
Molecular weight formula_weight	308.4 kDa
Source method src_method	man
Copy count entity_count	12

Entity 5 Entity 5 non-polymer

Description description	DECANE
Molecular weight formula_weight	142.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	31

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2vt4a_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamily	f.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family family	f.13.1.3 — Amine receptor-like

Domain ID domain_id	d2vt4b_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamily	f.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family family	f.13.1.3 — Amine receptor-like

Domain ID domain_id	d2vt4c_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamily	f.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family family	f.13.1.3 — Amine receptor-like

Domain ID domain_id	d2vt4d_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.13 — Class A G protein-coupled receptor (GPCR)-like
Superfamily Superfamily superfamily	f.13.1 — Class A G protein-coupled receptor (GPCR)-like
Family Family family	f.13.1.3 — Amine receptor-like

CATH v4.4 (4 domains)

Domain ID domain_id	2vt4A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily	10 — Rhodopsin 7-helix transmembrane proteins

Domain ID domain_id	2vt4B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily	10 — Rhodopsin 7-helix transmembrane proteins

Domain ID domain_id	2vt4C00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily	10 — Rhodopsin 7-helix transmembrane proteins

Domain ID domain_id	2vt4D00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily	10 — Rhodopsin 7-helix transmembrane proteins

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8. Citations (2)

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Unit-cell length a length_a	55.500 Å
Unit-cell length b length_b	86.800 Å
Unit-cell length c length_c	95.500 Å
Unit-cell angle α angle_alpha	67.60 °
Unit-cell angle β angle_beta	73.30 °
Unit-cell angle γ angle_gamma	85.80 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	45.100 Å
R factor r_factor	0.2150
R_work r_work	0.2120
R_free r_free	0.2680

fit	/app/data/saxs_computation/vt/2vt4/2vt4.fit
pddf	/app/data/pr_computation/vt/2vt4/2vt4.pr.out
profile	/app/data/saxs_computation/vt/2vt4/2vt4.dat