8YJP: Human apo GPR156

Cryo-EM structure of human apo GPR156. Determined by electron microscopy at 3.09 Å resolution. Released 5 Feb 2025.

Method: Electron microscopy
Resolution: 3.09 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,946
Mol. weight: 83.53 kDa
Ligands: CLR, MW9
Released: 5 Feb 2025

Explore 8YJP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8YJP contains 20 α-helices and 5 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: 10 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	24-33	10
α-helix	47-73	27
α-helix	78-82	5
α-helix	85-105	21
α-helix	115-149	35
α-helix	162-186	25
β-strand	191-201	11	1
β-strand	206	1	1
β-strand	209-216	8	1
α-helix	221-245	25
α-helix	252-255	4
α-helix	257-280	24
α-helix	285-318	34

Chain B: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	23-33	11
α-helix	49-73	25
α-helix	78-82	5
α-helix	85-105	21
α-helix	115-150	36
α-helix	162-186	25
β-strand	190-201	12	1
β-strand	206-217	12	1
α-helix	221-245	25
α-helix	252-255	4
α-helix	257-280	24
α-helix	285-318	34

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable G-protein coupled receptor 156	A, B	protein	346	Homo sapiens	Q8NFN8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8YJP_1 Probable G-protein coupled receptor 156 (chains A, B)
MEPEINCSELCDSFPGQELDRRPLHDLCKTTITSSHHSSKTISSLSPVLLGIVWTFLSCG
LLLILFFLAFTIHCRKNRIVKMSSPNLNIVTLLGSCLTYSSAYLFGIQDVLVGSSMETLI
QTRLSMLCIGTSLVFGPILGKSWRLYKVFTQRVPDKRVIIKDLQLLGLVAALLMADVILL
MTWVLTDPIQCLQILSVSMTVTGKDVSCTSTSTHFCASRYSDVWIALIWGCKGLLLLYGA
YLAGLTGHVSSPPVNQSLTIMVGVNLLVLAAGLLFVVTRYLHSWPNLVFGLTSGGIFVCT
TTINCFIFIPQLKQWKAFEEENQTIRRMAKYFSTPNKSFHTQYGEE

Ligands and cofactors

ID	Name	Formula	Copies
CLR	Cholesterol	C27 H46 O	9
MW9	(21R,24R,27S)-24,27,28-trihydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosp…	C42 H81 O10 P	4

Primary citation

Molecular insights into the activation mechanism of GPR156 in maintaining auditory function. Ma, X., Chen, L.N., Liao, M. et al. Nat Commun (2024) 15:10601-10601. DOI 10.1038/s41467-024-54681-5 · PubMed

Other PDB entries of the same protein (UniProt Q8NFN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8YK0 2.4 Å, Cryo-EM structure of human GPR156-Gi3 complex
8IEP 2.61 Å, Cryo-EM structure of GPR156C/D of G-protein free GPR156 (local refine)
8IEI 2.62 Å, Cryo-EM structure of GPR156A/B of G-protein free GPR156 (local refine)
8IEQ 2.73 Å, Cryo-EM structure of G-protein free GPR156
8IEB 3.03 Å, Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine)
8IED 3.33 Å, Cryo-EM structure of GPR156-miniGo-scFv16 complex

Browse structure collections

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