9CBL: Epinephrine-bound alpha-2A-adrenergic receptor

Cryo-EM structure of epinephrine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein. Determined by electron microscopy at 2.8 Å resolution. Released 11 Sept 2024.

Method: Electron microscopy
Resolution: 2.8 Å
Organisms: Rattus norvegicus, Bos taurus, Enterobacteria phage T4
Chains: 4
Atoms: 6,422
Mol. weight: 143.18 kDa
Ligands: ALE
Released: 11 Sept 2024

Explore 9CBL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CBL contains 32 α-helices and 36 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: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	17-20	4
α-helix	24-27	4
β-strand	34-39	6	1
α-helix	46-50	5
β-strand	185-190	6	1
β-strand	195-200	6	1
α-helix	212-215	4
β-strand	220-226	7	1
β-strand	233	1	2
β-strand	241	1	2
α-helix	247-254	8
β-strand	263-269	7	1
α-helix	271-278	8
α-helix	283-285	3
α-helix	302-308	7
β-strand	319-322	4	1
α-helix	331-350	20

Chain B: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	4-24	21
α-helix	30-33	4
α-helix	38-39	2
β-strand	49-51	3	3
β-strand	58-62	5	4
β-strand	71-74	4	4
β-strand	78-83	6	4
β-strand	88-94	7	4
β-strand	100-102	3	5
β-strand	111-116	6	5
β-strand	120-125	6	5
β-strand	134-140	7	5
β-strand	146-153	8	6
β-strand	156-161	6	6
β-strand	165-170	6	6
β-strand	175-180	6	6
β-strand	187-192	6	7
β-strand	198-203	6	7
β-strand	207-212	6	7
β-strand	217-223	7	7
β-strand	229-234	6	8
β-strand	240-245	6	8
β-strand	250-254	5	8
β-strand	260-264	5	8
β-strand	273-278	6	9
β-strand	284-289	6	9
β-strand	294-298	5	9
β-strand	304-307	4	9
β-strand	315-320	6	3
β-strand	327-331	5	3
β-strand	336-338	3	3

Chain G: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	10-22	13
α-helix	30-44	15
α-helix	45-47	3
α-helix	53-55	3

Chain R: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	48-73	26
α-helix	82-84	3
α-helix	85-96	12
α-helix	97-101	5
α-helix	102-111	10
α-helix	125-151	27
α-helix	155-157	3
α-helix	162-180	19
α-helix	209-216	8
α-helix	217-221	5
α-helix	223-225	3
α-helix	228-241	14
α-helix	386-414	29
α-helix	420-427	8
α-helix	429-440	12
α-helix	446-455	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(i) subunit alpha-1	A	protein	379	Rattus norvegicus	P10824 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	339	Bos taurus	P62871 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Bos taurus	P63212 (AlphaFold model)
Endolysin,Alpha-2A adrenergic receptor	R	protein	484	Enterobacteria phage T4, Homo sapiens	P00720, P08913

Sequence of entity 1 (A), FASTA

>9CBL_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A)
MGSSHHHHHHSSGLEVLFQGPHMASMGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVK
LLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDF
GDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYY
LNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGAQRSERKKWIHCF
EGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFE
EKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFV
FDAVTDVIIKNNLKDCGLF

Sequence of entity 2 (B), FASTA

>9CBL_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
SELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAM
HWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNIC
SIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFT
GHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAF
ATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALK
ADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>9CBL_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFSAIL

Sequence of entity 4 (R), FASTA

>9CBL_4 Endolysin,Alpha-2A adrenergic receptor (chains R)
MKTIIALSYIFCLVFADYKDDDDKNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSP
SLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRA
ALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGT
WDAYAAAGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFL
VSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRY
WSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEIND
QKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRQNREKRFTFVLAVVIGVFVVCWFP
FFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDASLE
VLFQ

Ligands and cofactors

ID	Name	Formula	Copies
ALE	L-epinephrine	C9 H13 N O3	1

Primary citation

Distinct binding conformations of epinephrine with alpha- and beta-adrenergic receptors. Lou, J.S., Su, M., Wang, J. et al. Exp Mol Med (2024) 56:1952-1966. DOI 10.1038/s12276-024-01296-x · PubMed

Other PDB entries of the same protein (UniProt P10824 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CIP 1.5 Å, Gi-alpha-1 subunit of guanine nucleotide-binding protein complexed with a GTP analogue
1SVS 1.5 Å, Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.
4N0D 1.55 Å, Crystal structure of the K345L variant of the Gi alpha1 subunit bound to GTPgammaS
5KDO 1.9 Å, Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and…
1AS0 2.0 Å, GTP-gamma-S bound G42V GIA1
1GIA 2.0 Å, Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis
1SVK 2.0 Å, Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP
4PAQ 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
4PAO 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
1FQJ 2.02 Å, Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma…
6M8H 2.07 Å, Crystal Structure of the R208Q mutant of G(i) subunit alpha-1
1BH2 2.1 Å, A326S mutant of an inhibitory alpha subunit

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