Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized ATP-dependent helicase MG140 (P47386)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized ATP-dependent helicase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P47386
- Type
- protein
- Length
- 1,113 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Uncharacterized ATP-dependent helicase MG140
- UniProt
- P47386
- Pockets
- 11 · best druggability 0.85
Structure
1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized ATP-dependent helicase MG140 | protein | 1113 | 51% helix, 15% strand | P47386 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.85 | 0.86 | 119 | empty |
| 2 | 110 | 0.63 | 0.88 | 22 | empty |
| 3 | 328 | 0.62 | 0.79 | 40 | empty |
| 4 | 339 | 0.59 | 0.77 | 32 | empty |
| 5 | 271 | 0.59 | 0.78 | 42 | empty |
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 P47386
- Elsewhere: UniProt P47386 · AlphaFold DB P47386
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