Research workbench
Cryo-EM structure of GPR158 coupled to the RGS7-GBETA5 complex
Analyse Cryo-EM structure of GPR158 coupled to the RGS7-GBETA5 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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.
| Volume (ų) | 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 Ų buried · 18 hydrogen bonds · protein-protein
- C–A · 1658 Ų buried · 7 hydrogen bonds · protein-protein
- B–A · 1370 Ų buried · 5 hydrogen bonds · protein-protein
- C–B · 242 Ų 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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