2Y01: Beta-1 adrenergic receptor

Name: PDB 2Y01: Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist dobutamine (crystal DOB102)
Published: 2011-03-30
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: receptor

Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist dobutamine (crystal DOB102). Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Mar 2011.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: MELEAGRIS GALLOPAVO
Chains: 2
Atoms: 5,053
Mol. weight: 78.23 kDa
Ligands: Y01, 2CV, Y00
Released: 30 Mar 2011

Explore 2Y01 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y01 contains 36 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	34-67	34
α-helix	70-72	3
α-helix	76-89	14
α-helix	90-94	5
α-helix	95-104	10
α-helix	111-144	34
α-helix	146-152	7
α-helix	155-178	24
α-helix	187-193	7
α-helix	205-212	8
α-helix	213-217	5
α-helix	218-235	18
α-helix	279-315	37
α-helix	322-334	13
α-helix	335-337	3
α-helix	338-342	5
α-helix	343-345	3
α-helix	347-356	10

Chain B: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	34-68	35
α-helix	70-72	3
α-helix	76-89	14
α-helix	90-94	5
α-helix	95-104	10
α-helix	111-144	34
α-helix	148-152	5
α-helix	155-178	24
α-helix	187-194	8
α-helix	205-212	8
α-helix	213-217	5
α-helix	218-237	20
α-helix	278-315	38
α-helix	322-334	13
α-helix	335-337	3
α-helix	338-342	5
α-helix	343-345	3
α-helix	347-356	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-1 adrenergic receptor	A, B	protein	315	MELEAGRIS GALLOPAVO	P07700 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2Y01_1 BETA-1 ADRENERGIC RECEPTOR (chains A, B)
MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVV
GLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQ
SLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIA
SSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKTSRVMLMREHKALKTLGIIMGV
FTLCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLA
FPRKADRRLHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
Y01	Cholesterol hemisuccinate	C31 H50 O4	4
2CV	Hega-10	C18 H37 N O7	10
Y00	Dobutamine	C18 H23 N O3	2

Primary citation

The Structural Basis for Agonist and Partial Agonist Action on a Beta1-Adrenergic Receptor. Warne, A., Moukhametzianov, R., Baker, J.G. et al. Nature (2011) 469:241. DOI 10.1038/NATURE09746 · PubMed

Other PDB entries of the same protein (UniProt P07700 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4BVN 2.1 Å, Ultra-thermostable beta1-adrenoceptor with cyanopindolol bound
4AMJ 2.3 Å, Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist…
5A8E 2.4 Å, thermostabilised beta1-adrenoceptor with rationally designed inverse agonist…
2Y00 2.5 Å, Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist…
6H7N 2.5 Å, Activated turkey BETA1 adrenoceptor with bound partial agonist xamoterol and nanobody…
8DCS 2.5 Å, Cryo-EM structure of cyanopindolol-bound beta1-adrenergic receptor in complex with…
2Y02 2.6 Å, Turkey BETA1 adrenergic receptor with stabilising mutations and bound agonist carmoterol
7JJO 2.6 Å, Structural Basis of the Activation of Heterotrimeric Gs-protein by Isoproterenol-bound…
8DCR 2.6 Å, Cryo-EM structure of dobutamine-bound beta1-adrenergic receptor in complex with…
2VT4 2.7 Å, Turkey BETA1 adrenergic receptor with stabilising mutations and bound cyanopindolol
3ZPR 2.7 Å, Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl)…
6H7L 2.7 Å, Activated turkey BETA1 adrenoceptor with bound partial agonist dobutamine and nanobody…

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