8IEP: GPR156C/D of G-protein free GPR156

Cryo-EM structure of GPR156C/D of G-protein free GPR156 (local refine). Determined by electron microscopy at 2.61 Å resolution. Released 14 Feb 2024.

Method: Electron microscopy
Resolution: 2.61 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,431
Mol. weight: 132.78 kDa
Ligands: A1LYA
Released: 14 Feb 2024

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

Secondary structure: helices and β-sheets

8IEP contains 16 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 C: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	47-73	27
α-helix	78-81	4
α-helix	85-104	20
α-helix	116-149	34
α-helix	162-186	25
β-strand	191-201	11	1
β-strand	206-216	11	1
α-helix	221-245	25
α-helix	258-280	23
α-helix	285-331	47

Chain D: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	47-73	27
α-helix	78-82	5
α-helix	85-104	20
α-helix	116-148	33
α-helix	162-186	25
β-strand	190-201	12	1
β-strand	206-217	12	1
α-helix	221-245	25
α-helix	257-280	24
α-helix	285-331	47

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable G-protein coupled receptor 156	C, D	protein	598	Homo sapiens	Q8NFN8 (AlphaFold model)

Sequence of entity 1 (C, D), FASTA

>8IEP_1 Probable G-protein coupled receptor 156 (chains C, D)
MEPEINCSELCDSFPGQELDRRPLHDLCKTTITSSHHSSKTISSLSPVLLGIVWTFLSCG
LLLILFFLAFTIHCRKNRIVKMSSPNLNIVTLLGSCLTYSSAYLFGIQDVLVGSSMETLI
QTRLSMLCIGTSLVFGPILGKSWRLYKVFTQRVPDKRVIIKDLQLLGLVAALLMADVILL
MTWVLTDPIQCLQILSVSMTVTGKDVSCTSTSTHFCASRYSDVWIALIWGCKGLLLLYGA
YLAGLTGHVSSPPVNQSLTIMVGVNLLVLAAGLLFVVTRYLHSWPNLVFGLTSGGIFVCT
TTINCFIFIPQLKQWKAFEEENQTIRRMAKYFSTPNKSFHTQYGEEENCHPRGEKSSMER
LLTEKNAVIESLQEQVNNAKEKIVRLMSAECTYDLPEGAAPPASSPNKDVQAVASVHTLA
AAQGPSGHLSDFQNDPGMAARDSQCTSGPSSYAQSLEGPGKDSSFSPGKEEKISDSKDFS
DHLDSGCSQKPWTEQSLGPERGDQVPMNPSQSLLPERGGSDPQRQRHLENSEEPPERRSR
VSSVIREKLQEVLQDLGSGSGSGRGRGGSENLYFQGGSGSGGDYKDDDDKDYKDDDDK

Ligands and cofactors

ID	Name	Formula	Copies
A1LYA	[(2R)-3-[(E)-hexadec-9-enoyl]oxy-2-octadecanoyloxy-propyl]…	C42 H82 N O8 P	2

Primary citation

Constitutive activation mechanism of a class C GPCR. Shin, J., Park, J., Jeong, J. et al. Nat Struct Mol Biol (2024) 31:678-687. DOI 10.1038/s41594-024-01224-7 · 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
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)
8YJP 3.09 Å, Cryo-EM structure of human apo GPR156
8IED 3.33 Å, Cryo-EM structure of GPR156-miniGo-scFv16 complex

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