Research workbench
AlphaFold monomer V2.0 prediction for repellent protein 1 (Q99109)
Analyse AlphaFold monomer V2.0 prediction for repellent protein 1 (Q99109) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99109
- Type
- protein
- Length
- 652 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Repellent protein 1
- UniProt
- Q99109
- Pockets
- 4 · best druggability 0.86
Structure
1 distinct chain · 1% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Repellent protein 1 | protein | 652 | 1% helix, 38% strand | Q99109 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1044 | 0.86 | 0.88 | 126 | empty |
| 2 | 167 | 0.67 | 0.87 | 27 | empty |
| 3 | 356 | 0.55 | 0.74 | 37 | empty |
| 4 | 67 | 0.49 | 0.83 | 20 | 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 Q99109
- Elsewhere: UniProt Q99109 · AlphaFold DB Q99109
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