7F83: Receptor

Crystal Structure of a receptor in Complex with inverse agonist. Determined by X-ray diffraction at 2.94 Å resolution. Released 19 Jan 2022.

Method: X-ray diffraction
Resolution: 2.94 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 2
Atoms: 6,227
Mol. weight: 97.53 kDa
Ligands: 1KQ, OLC
Released: 19 Jan 2022

Explore 7F83 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7F83 contains 35 α-helices and 4 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	40-70	31
α-helix	72-74	3
α-helix	77-103	27
α-helix	112-146	35
α-helix	157-181	25
β-strand	182-183	2	1
β-strand	199-200	2	1
α-helix	202-207	6
α-helix	209-226	18
α-helix	227-232	6
α-helix	233-239	7
α-helix	1005-1022	18
α-helix	1028-1046	19
α-helix	1051-1053	3
α-helix	1061-1085	25
α-helix	1089-1106	18
α-helix	1108-1110	3
α-helix	258-288	31
α-helix	295-326	32
α-helix	328-338	11

Chain B: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	40-70	31
α-helix	77-104	28
α-helix	112-146	35
α-helix	159-175	17
α-helix	178-181	4
β-strand	182-183	2	2
β-strand	199-200	2	2
α-helix	202-205	4
α-helix	209-226	18
α-helix	227-231	5
α-helix	232-239	8
α-helix	1005-1024	20
α-helix	1032-1046	15
α-helix	1051-1053	3
α-helix	1064-1085	22
α-helix	1092-1107	16
α-helix	258-288	31
α-helix	296-326	31
α-helix	328-335	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth hormone secretagogue receptor type 1,Soluble cytochrome b562	A, B	protein	416	Homo sapiens, Escherichia coli	Q92847 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7F83_1 Growth hormone secretagogue receptor type 1,Soluble cytochrome b562 (chains A, B)
LQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFL
CMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYAKVLTITALSVERYFAICFPLRAKVV
VTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHEQGTDPWDTNECRPTEFAVRSGLLTVMV
WVSSIFFFLPVFCLTVLYSLIGRKLWRRRGGTTMADLEDNWETLNDNLKVIEKADNAAQV
KDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKE
AQAAAEQLKTTRNAYIQKYLLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEP
GSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
1KQ	2-(2-methylimidazo[2,1-b][1,3]thiazol-6-yl)-1-[2-[(1R)-5-(6-methylpyrimidin-4-y…	C29 H32 N6 O S	2
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	6

Primary citation

Molecular mechanism of agonism and inverse agonism in ghrelin receptor. Qin, J., Cai, Y., Xu, Z. et al. Nat Commun (2022) 13:300-300. DOI 10.1038/s41467-022-27975-9 · PubMed

Other PDB entries of the same protein (UniProt Q92847 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9UY3 2.52 Å, Anamorelin bound growth hormone secretagogue receptor in complex with Gq
9V2N 2.63 Å, Macimorelin bound growth hormone secretagogue receptor in complex with Gq
7NA7 2.7 Å, Structures of human ghrelin receptor-Gi complexes with ghrelin and a synthetic agonist
7NA8 2.7 Å, Structures of human ghrelin receptor-Gi complexes with ghrelin and a synthetic agonist
7W2Z 2.8 Å, Cryo-EM structure of the ghrelin-bound human ghrelin receptor-Go complex
7F9Y 2.9 Å, ghrelin-bound ghrelin receptor in complex with Gq
8JSR 2.9 Å, Cryo-EM structure of the anamorelin-bound ghrelin receptor and Gq complex
7F9Z 3.2 Å, GHRP-6-bound ghrelin receptor in complex with Gq
6KO5 3.3 Å, Complex structure of Ghrelin receptor with Fab
8ZZO Structural Model of Ghrelin Bound to its G Protein-Coupled Receptor

Browse structure collections

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