Research workbench
AlphaFold monomer V2.0 prediction for zinc finger and btb domain- containing protein 24 (Q3B725)
Analyse AlphaFold monomer V2.0 prediction for zinc finger and btb domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3B725
- Type
- protein
- Length
- 705 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Zinc finger and btb domain-containing protein 24
- UniProt
- Q3B725
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 27% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger and btb domain-containing protein 24 | protein | 705 | 27% helix, 5% strand | Q3B725 |
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 | 433 | 0.64 | 0.77 | 45 | empty |
| 2 | 174 | 0.60 | 0.82 | 30 | empty |
| 3 | 125 | 0.40 | 0.75 | 23 | empty |
Modifications
Observed in the structure: 2 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 Q3B725
- Elsewhere: UniProt Q3B725 · AlphaFold DB Q3B725
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