6TKO: Beta-1 adrenergic receptor

Phosphorylated turkey beta1 adrenoceptor with bound agonist formoterol coupled to arrestin-2 in lipid nanodisc. Determined by electron microscopy at 3.3 Å resolution. Released 17 Jun 2020.

Method: Electron microscopy
Resolution: 3.3 Å
Organisms: Meleagris gallopavo, Homo sapiens, Phage display vector pTDisp
Chains: 4
Atoms: 8,085
Mol. weight: 133.59 kDa
Ligands: H98
Released: 17 Jun 2020

Explore 6TKO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TKO contains 35 α-helices and 70 β-strands across 4 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: 15 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	45-68	24
α-helix	75-89	15
α-helix	90-94	5
α-helix	95-104	10
α-helix	111-143	33
α-helix	146-152	7
α-helix	155-179	25
α-helix	187-194	8
α-helix	205-212	8
α-helix	213-217	5
α-helix	218-241	24
α-helix	281-315	35
α-helix	322-343	22
α-helix	347-357	11
β-strand	1361-1364	4	1
α-helix	1365-1367	3

Chain B: 12 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	7-12	6	1
β-strand	19-22	4	1
β-strand	26-28	3	2
α-helix	34-35	2
β-strand	36	1	3
β-strand	39-42	4	1
β-strand	52-62	11	4
β-strand	76-87	12	4
α-helix	90	1
α-helix	96-98	3
α-helix	99-108	10
β-strand	112-115	4	1
β-strand	118	1	3
α-helix	119-120	2
β-strand	127-129	3	4
α-helix	139	1
β-strand	140-151	12	4
β-strand	165-168	4	4
β-strand	169-171	3	2
α-helix	178-180	3
β-strand	183-187	5	5
β-strand	197-203	7	5
β-strand	207-208	2	6
β-strand	214-218	5	5
β-strand	220-222	3	5
β-strand	228-241	14	7
β-strand	247-258	12	7
β-strand	262	1	7
β-strand	266-267	2	5
β-strand	270-274	5	5
α-helix	281-283	3
β-strand	288-290	3	4
α-helix	297-298	2
β-strand	300	1	4
α-helix	301-304	4
α-helix	306-307	2
β-strand	319-329	11	7
β-strand	342-349	8	7
β-strand	350-351	2	6
α-helix	353-357	5

Chain H: 2 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	8
β-strand	15	1	9
β-strand	20-28	9	8
β-strand	35-42	8	10
β-strand	48-55	8	10
β-strand	60-63	4	10
β-strand	71-76	6	8
β-strand	81-87	7	8
α-helix	91-93	3
β-strand	95-103	9	10
β-strand	113	1	10
β-strand	117-119	3	10
β-strand	121	1	9
β-strand	130-134	5	11
β-strand	147-155	9	11
β-strand	161-164	4	12
β-strand	174-175	2	11
α-helix	176-178	3
β-strand	179-180	2	11
β-strand	186-193	8	11
β-strand	205-210	6	12
β-strand	215-220	6	12

Chain L: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	13
β-strand	11-14	4	14
β-strand	20-26	7	13
β-strand	35-39	5	15
α-helix	44	1
β-strand	45-50	6	15
β-strand	54-55	2	15
α-helix	56	1
β-strand	63-67	5	13
β-strand	71-76	6	13
α-helix	81-83	3
β-strand	86-90	5	15
α-helix	97	1
β-strand	100	1	13
β-strand	104-107	4	14
β-strand	112	1	16
β-strand	115-119	5	17
α-helix	123-128	6
β-strand	130-140	11	17
β-strand	141	1	16
β-strand	146-150	5	18
β-strand	155-156	2	18
β-strand	160-165	6	17
β-strand	174-183	10	17
α-helix	184-189	6
β-strand	192-198	7	18
β-strand	206-211	6	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-1 adrenergic receptor	A	protein	328	Meleagris gallopavo	P07700 (AlphaFold model)
Beta-arrestin-1	B	protein	418	Homo sapiens	P49407 (AlphaFold model)
Fab30 heavy chain	H	protein	237	Phage display vector pTDisp
Fab30 light chain	L	protein	215	Phage display vector pTDisp

Sequence of entity 1 (A), FASTA

>6TKO_1 Beta-1 adrenergic receptor (chains A)
GAELLSQQWEAGCSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVVG
LLVVPFGATLVCRGTWLWGSFLCELWTSLDVLCVTASIWTLCVIAIDRYLAITSPFRYQS
LMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIAS
SIISFYIPLLIMIFVYLRVYREAKEQIRKIDRASKRKTSRVMAMREHKALKTLGIIMGVF
TLCWLPFFLVNIVNVFNRDLVPKWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLAA
RGRPLPETGGGDESATTASSSLAKDTSS

Sequence of entity 2 (B), FASTA

>6TKO_2 Beta-arrestin-1 (chains B)
GGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCA
FRYGREDCDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP
PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIEKVQYAPERPGP
QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD
ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL
ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEP
PHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR

Sequence of entity 3 (H), FASTA

>6TKO_3 Fab30 heavy chain (chains H)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH

Sequence of entity 4 (L), FASTA

>6TKO_4 Fab30 light chain (chains L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Ligands and cofactors

ID	Name	Formula	Copies
H98	~{N}-[5-[(1~{R})-2-[[(2~{R})-1-(4-methoxyphenyl)propan-2-yl]amino]-1-oxidanyl-e…	C19 H24 N2 O4	1

Primary citation

Molecular basis of beta-arrestin coupling to formoterol-bound beta1-adrenoceptor. Lee, Y., Warne, T., Nehme, R. et al. Nature (2020) 583:862-866. DOI 10.1038/s41586-020-2419-1 · 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
3ZPR 2.7 Å, Thermostabilised turkey beta1 adrenergic receptor with 4-methyl-2-(piperazin-1-yl)…

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