Research workbench
AlphaFold monomer V2.0 prediction for zinc finger protein interacting with ribonucleoprotein K (Q3SY52)
Analyse AlphaFold monomer V2.0 prediction for zinc finger protein interacting with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3SY52
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Zinc finger protein interacting with ribonucleoprotein K
- UniProt
- Q3SY52
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 34% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger protein interacting with ribonucleoprotein K | protein | 487 | 34% helix, 7% strand | Q3SY52 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1006 | 0.77 | 0.79 | 74 | empty |
| 2 | 131 | 0.45 | 0.77 | 18 | empty |
| 3 | 59 | 0.27 | 0.73 | 14 | empty |
| 4 | 55 | 0.25 | 0.72 | 12 | 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 Q3SY52
- Elsewhere: UniProt Q3SY52 · AlphaFold DB Q3SY52
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