Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylinositol N-acetylglucosaminyltransferase subunit C (Q5PQQ4)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylinositol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5PQQ4
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1C6d74B24246Fb79541e3b0466c2b0D0b51a2553
- Molecule
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- UniProt
- Q5PQQ4
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol N-acetylglucosaminyltransferase subunit C | protein | 297 | 67% helix, 1% strand | Q5PQQ4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 521 | 0.67 | 0.78 | 49 | empty |
| 2 | 134 | 0.49 | 0.79 | 24 | empty |
| 3 | 185 | 0.46 | 0.74 | 22 | empty |
| 4 | 120 | 0.42 | 0.76 | 19 | 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 Q5PQQ4
- Elsewhere: UniProt Q5PQQ4 · AlphaFold DB Q5PQQ4
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