Research workbench
cryo-EM structure of apo GPR158
Analyse cryo-EM structure of apo GPR158 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EWL
- Type
- protein
- Length
- 994 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.52
- Source
- Homo sapiens
- Molecule
- Probable G-protein coupled receptor 158
- UniProt
- Q5T848
- Pockets
- 16 · best druggability 0.79
Structure
electron microscopy · resolution 3.52 · 2 distinct chains · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable G-protein coupled receptor 158 | protein | 499 | 47% helix, 13% strand | Q5T848 |
| B | Probable G-protein coupled receptor 158 | protein | 495 | 45% helix, 12% strand | Q5T848 |
Pockets
16 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1126 | 0.79 | 0.80 | 52 | empty |
| 2 | 95 | 0.76 | 0.97 | 23 | empty |
| 3 | 646 | 0.74 | 0.81 | 82 | empty |
| 4 | 776 | 0.73 | 0.78 | 84 | empty |
| 5 | 71 | 0.72 | 0.96 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1808 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
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 Q5T848
- Elsewhere: RCSB PDB 7EWL · PDBe 7EWL · UniProt Q5T848
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