Research workbench
AlphaFold monomer V2.0 prediction for protein nuclear fusion defective 5, mitochondrial (Q8LEZ4)
Analyse AlphaFold monomer V2.0 prediction for protein nuclear fusion defective 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8LEZ4
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x66cc7a0eB7D43468C5dDa46c4E407dc0C1A1C67C
- Molecule
- Protein nuclear fusion defective 5, mitochondrial
- UniProt
- Q8LEZ4
- Pockets
- 4 · best druggability 0.39
Structure
1 distinct chain · 51% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein nuclear fusion defective 5, mitochondrial | protein | 372 | 51% helix, 1% strand | Q8LEZ4 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.39 | 0.73 | 17 | empty |
| 2 | 76 | 0.32 | 0.74 | 8 | empty |
| 3 | 78 | 0.29 | 0.72 | 13 | empty |
| 4 | 58 | 0.28 | 0.73 | 13 | 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 Q8LEZ4
- Elsewhere: UniProt Q8LEZ4 · AlphaFold DB Q8LEZ4
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