Research workbench
AlphaFold monomer V2.0 prediction for protein fem-1 homolog a (Q4V890)
Analyse AlphaFold monomer V2.0 prediction for protein fem-1 homolog a (Q4V890) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4V890
- Type
- protein
- Length
- 654 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Protein fem-1 homolog a
- UniProt
- Q4V890
- Pockets
- 7 · best druggability 0.57
Structure
1 distinct chain · 56% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fem-1 homolog a | protein | 654 | 56% helix, 2% strand | Q4V890 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.57 | 0.77 | 39 | empty |
| 2 | 133 | 0.51 | 0.80 | 18 | empty |
| 3 | 99 | 0.37 | 0.75 | 14 | empty |
| 4 | 71 | 0.37 | 0.78 | 16 | empty |
| 5 | 70 | 0.33 | 0.75 | 13 | 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 Q4V890
- Elsewhere: UniProt Q4V890 · AlphaFold DB Q4V890
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