2Y00: Beta-1 adrenergic receptor

Name: PDB 2Y00: Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist dobutamine (crystal DOB92)
Published: 2011-01-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: receptor

Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist dobutamine (crystal DOB92). Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Jan 2011.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: MELEAGRIS GALLOPAVO
Chains: 2
Atoms: 5,052
Mol. weight: 78.25 kDa
Ligands: Y00, 2CV, Y01
Released: 12 Jan 2011

Explore 2Y00 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y00 contains 37 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: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	34-66	33
α-helix	70-72	3
α-helix	75-89	15
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	187-194	8
α-helix	205-212	8
α-helix	213-217	5
α-helix	218-235	18
α-helix	279-315	37
α-helix	317-319	3
α-helix	322-334	13
α-helix	335-337	3
α-helix	338-342	5
α-helix	343-345	3
α-helix	347-357	11

Chain B: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	34-66	33
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	218-237	20
α-helix	277-315	39
α-helix	322-334	13
α-helix	335-337	3
α-helix	338-342	5
α-helix	343-345	3
α-helix	347-357	11

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

>2Y00_1 BETA-1 ADRENERGIC RECEPTOR (chains A, B)
MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVV
GLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQ
SLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIA
SSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKTSRVMLMREHKALKTLGIIMGV
FTLCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLA
FPRKADRRLHHHHHH

Ligands and cofactors

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

Water and common crystallization additives (NA) are not listed.

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…
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…
2Y01 2.6 Å, Turkey BETA1 adrenergic receptor with stabilising mutations and bound partial agonist…
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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