Research workbench
AlphaFold monomer V2.0 prediction for zinc finger protein lin-13 (Q11107)
Analyse AlphaFold monomer V2.0 prediction for zinc finger protein lin-13 (Q11107) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q11107
- Type
- protein
- Length
- 2,248 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x28e51F615E58598362D09182b4f56f5cAD52f49a
- Molecule
- Zinc finger protein lin-13
- UniProt
- Q11107
- Pockets
- 20 · best druggability 0.70
Structure
1 distinct chain · 27% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger protein lin-13 | protein | 2248 | 27% helix, 9% strand | Q11107 |
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.70 | 0.81 | 55 | empty |
| 2 | 689 | 0.67 | 0.75 | 50 | empty |
| 3 | 592 | 0.67 | 0.76 | 57 | empty |
| 4 | 334 | 0.66 | 0.80 | 46 | empty |
| 5 | 201 | 0.46 | 0.74 | 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 Q11107
- Elsewhere: UniProt Q11107 · AlphaFold DB Q11107
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