Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized membrane protein F35D11.3 (Q20035)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized membrane protein F35D11.3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q20035
- Type
- protein
- Length
- 617 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Uncharacterized membrane protein F35D11.3
- UniProt
- Q20035
- Pockets
- 8 · best druggability 0.57
Structure
1 distinct chain · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized membrane protein F35D11.3 | protein | 617 | 47% helix, 8% strand | Q20035 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.57 | 0.76 | 43 | empty |
| 2 | 204 | 0.56 | 0.79 | 27 | empty |
| 3 | 226 | 0.55 | 0.78 | 29 | empty |
| 4 | 129 | 0.53 | 0.81 | 30 | empty |
| 5 | 77 | 0.41 | 0.79 | 22 | 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 Q20035
- Elsewhere: UniProt Q20035 · AlphaFold DB Q20035
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