3ZPR: Beta-1 adrenergic receptor

Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl) quinoline bound. Determined by X-ray diffraction at 2.7 Å resolution. Released 3 Apr 2013.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: MELEAGRIS GALLOPAVO
Chains: 2
Atoms: 4,952
Mol. weight: 77.41 kDa
Ligands: 2CV, 3WC, Y01
Released: 3 Apr 2013

Explore 3ZPR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ZPR 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	33-68	36
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	218-236	19
α-helix	282-315	34
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	33-68	36
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	218-236	19
α-helix	272-274	3
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

>3ZPR_1 BETA-1 ADRENERGIC RECEPTOR (chains A, B)
MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVV
GLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQ
SLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIA
SSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKTSRVMLMREHKALKTLGIIMGV
FTLCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLA
FPRKADRRLHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
2CV	Hega-10	C18 H37 N O7	8
3WC	4-methyl-2-(piperazin-1-yl) quinoline	C14 H17 N3	2
Y01	Cholesterol hemisuccinate	C31 H50 O4	4

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

Primary citation

Biophysical Fragment Screening of the Beta1-Adrenergic Receptor: Identification of High Affinity Aryl Piperazine Leads Using Structure-Based Drug Design. Christopher, J., Brown, J., Dore, A. et al. J Med Chem (2013) 56:3446. DOI 10.1021/JM400140Q · 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…
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
6H7L 2.7 Å, Activated turkey BETA1 adrenoceptor with bound partial agonist dobutamine and nanobody…

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