MolNFT v1 · #187504 · protein

Cryo-EM structure of GPR158 coupled to the RGS7-GBETA5 complex

7SHF · Isoform 2 of regulator of G-protein signaling 7: “Cryo-EM structure of GPR158 coupled to the RGS7-GBETA5 complex”. Electron microscopy, 3 ligands (CLR, EIJ, PEE), 19 pockets (best druggability 0.86). MolNFT v1 #187504 on GenesisL1…

PDB: 7SHF
Type: protein
Length: 1,326 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 2 of regulator of G-protein signaling 7; Guanine nucleotide-binding protein…
UniProt: P49802, P62881, Q5T848
Ligands: CLR, EIJ, PEE
Pockets: 19 · best druggability 0.86

Structure

electron microscopy · 4 distinct chains · 41% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Isoform 2 of regulator of G-protein signaling 7	protein	400	58% helix, 5% strand	P49802
D	Guanine nucleotide-binding protein subunit beta-5	protein	346	10% helix, 42% strand	P62881
B	G-protein coupled receptor 158	protein	284	54% helix, 1% strand	Q5T848
A	G-protein coupled receptor 158	protein	296	43% helix, 4% strand	Q5T848

Ligands and binding sites

CLR · Cholesterol · ligand · 22 copies · chains B, A, C
EIJ · (2S)-1-{[(S)-hydroxy{[(1s,2r,3r,4r,5s,6s)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-3-(octadecanoyloxy)propan-2-yl (5E,8E,11E,14E)-icosa-5, 8,11,14-tetraenoate · ligand · chains B, A
PEE · 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine · ligand · chains B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1074	0.86	0.87	116	empty
2	880	0.80	0.82	45	EIJ, PEE
3	290	0.78	0.89	51	empty
4	95	0.75	0.96	24	empty
5	186	0.68	0.87	32	empty

Interfaces

4 interfaces between chains.

C–D · 4138 Å² buried · 18 hydrogen bonds · protein-protein
C–A · 1658 Å² buried · 7 hydrogen bonds · protein-protein
B–A · 1370 Å² buried · 5 hydrogen bonds · protein-protein
C–B · 242 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7SHF · Cryo-EM structure of GPR158 coupled to the RGS7-Gbeta5 complex · the same entry in another collection · chain A against A, TM-score 1.00
P49802 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 7 (P49802) · a predicted model of the same protein · chain C against A, TM-score 0.96
P62881 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein subunit beta-5… · a predicted model of the same protein · chain D against A, TM-score 0.95
Q5T848 · AlphaFold monomer V2.0 prediction for probable G-protein coupled receptor 158 (Q5T848) · a predicted model of the same protein · chain B against A, TM-score 0.90

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P49802
Every structure of UniProt P62881
Every structure of UniProt Q5T848
Elsewhere: RCSB PDB 7SHF · PDBe 7SHF · UniProt P49802 · UniProt P62881 · UniProt Q5T848

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