Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein SFH5 (Q75BM4)
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
- Q75BM4
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb8D3B450AC50e83021eF2fc524AAC2745D922097
- Molecule
- Phosphatidylinositol transfer protein SFH5
- UniProt
- Q75BM4
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol transfer protein SFH5 | protein | 295 | 54% helix, 12% strand | Q75BM4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.81 | 0.90 | 56 | empty |
| 2 | 197 | 0.54 | 0.78 | 31 | empty |
| 3 | 87 | 0.43 | 0.79 | 17 | empty |
| 4 | 98 | 0.40 | 0.76 | 16 | 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 Q75BM4
- Elsewhere: UniProt Q75BM4 · AlphaFold DB Q75BM4
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