Research workbench
AlphaFold monomer V2.0 prediction for myelin proteolipid protein (P47790)
Analyse AlphaFold monomer V2.0 prediction for myelin proteolipid protein (P47790) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P47790
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Myelin proteolipid protein
- UniProt
- P47790
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 79% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myelin proteolipid protein | protein | 277 | 79% helix, 3% strand | P47790 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.74 | 0.85 | 39 | empty |
| 2 | 76 | 0.39 | 0.77 | 14 | empty |
| 3 | 109 | 0.33 | 0.72 | 16 | empty |
| 4 | 55 | 0.27 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P47790
- Elsewhere: UniProt P47790 · AlphaFold DB P47790
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