Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized protein AF_1001 (O29261)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized protein AF_1001 (O29261) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O29261
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Uncharacterized protein AF_1001
- UniProt
- O29261
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 13% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein AF_1001 | protein | 194 | 13% helix, 43% strand | O29261 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.56 | 0.75 | 32 | empty |
| 2 | 60 | 0.43 | 0.82 | 14 | empty |
| 3 | 101 | 0.37 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 1 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 O29261
- Elsewhere: UniProt O29261 · AlphaFold DB O29261
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