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AlphaFold monomer V2.0 prediction for uncharacterized 10.9 kda protein in seca 5'REGION (Q01572)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized 10.9 kda protein in seca… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q01572
- Type
- protein
- Length
- 93 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Uncharacterized 10.9 kda protein in seca 5'REGION
- UniProt
- Q01572
- Pockets
- 3 · best druggability 0.62
Structure
1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized 10.9 kda protein in seca 5'REGION | protein | 93 | 70% helix, 0% strand | Q01572 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.62 | 0.83 | 23 | empty |
| 2 | 159 | 0.58 | 0.81 | 29 | empty |
| 3 | 74 | 0.43 | 0.80 | 13 | 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 Q01572
- Elsewhere: UniProt Q01572 · AlphaFold DB Q01572
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