Research workbench
AlphaFold monomer V2.0 prediction for dynamin-like protein a (Q55F94)
Analyse AlphaFold monomer V2.0 prediction for dynamin-like protein a (Q55F94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q55F94
- Type
- protein
- Length
- 880 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Dynamin-like protein a
- UniProt
- Q55F94
- Pockets
- 8 · best druggability 0.64
Structure
1 distinct chain · 56% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dynamin-like protein a | protein | 880 | 56% helix, 6% strand | Q55F94 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.64 | 0.80 | 33 | empty |
| 2 | 240 | 0.57 | 0.79 | 34 | empty |
| 3 | 214 | 0.54 | 0.78 | 33 | empty |
| 4 | 140 | 0.44 | 0.76 | 21 | empty |
| 5 | 150 | 0.41 | 0.74 | 25 | 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 Q55F94
- Elsewhere: UniProt Q55F94 · AlphaFold DB Q55F94
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