Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein SFH5 (A7EXH9)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7EXH9
- Type
- protein
- Length
- 413 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Phosphatidylinositol transfer protein SFH5
- UniProt
- A7EXH9
- Pockets
- 3 · best druggability 0.82
Structure
1 distinct chain · 37% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol transfer protein SFH5 | protein | 413 | 37% helix, 9% strand | A7EXH9 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 971 | 0.82 | 0.83 | 85 | empty |
| 2 | 104 | 0.35 | 0.74 | 15 | empty |
| 3 | 58 | 0.28 | 0.74 | 15 | 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 A7EXH9
- Elsewhere: UniProt A7EXH9 · AlphaFold DB A7EXH9
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