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Cryo-EM structure of human GPR158 in complex with RGS7-GBETA5 in a 2:2:2 ratio

Analyse Cryo-EM structure of human GPR158 in complex with RGS7-GBETA5 in a 2:2:2 ratio in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EWR
Type: protein
Length: 2,516 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulator of G-protein signaling 7; Guanine nucleotide-binding protein subunit beta-5…
UniProt: P49802, O14775, Q5T848
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 6 distinct chains · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Regulator of G-protein signaling 7	protein	381	56% helix, 3% strand	P49802
F	Guanine nucleotide-binding protein subunit beta-5	protein	319	2% helix, 37% strand	O14775
A	Probable G-protein coupled receptor 158	protein	577	50% helix, 8% strand	Q5T848
B	Probable G-protein coupled receptor 158	protein	504	47% helix, 12% strand	Q5T848
C	Regulator of G-protein signaling 7	protein	396	57% helix, 3% strand	P49802
D	Guanine nucleotide-binding protein subunit beta-5	protein	339	7% helix, 35% strand	O14775

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.87	0.88	119	empty
2	1026	0.86	0.87	106	empty
3	1053	0.86	0.87	125	empty
4	975	0.81	0.83	119	empty
5	1038	0.80	0.81	64	empty

Interfaces

5 interfaces between chains.

C–D · 3579 Å² buried · 21 hydrogen bonds · protein-protein
E–F · 3143 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1835 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 1324 Å² buried · 2 hydrogen bonds · protein-protein
E–A · 166 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

7EWR · Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio · the same entry in another collection · chain D against D, TM-score 1.00
O14775 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein subunit beta-5… · a predicted model of the same protein · chain F against A, TM-score 0.97
P49802 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 7 (P49802) · a predicted model of the same protein · chain E against A, TM-score 0.97
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 0.83

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 O14775
Every structure of UniProt Q5T848
Elsewhere: RCSB PDB 7EWR · PDBe 7EWR · UniProt P49802 · UniProt O14775 · UniProt Q5T848

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