Research workbench
AlphaFold monomer V2.0 prediction for polypeptide N-acetylgalactosaminyltransferase 17 (Q7TT15)
Analyse AlphaFold monomer V2.0 prediction for polypeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7TT15
- Type
- protein
- Length
- 598 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x91Dc148ab08c1AB493A2D909C4D467a056F6E73d
- Molecule
- Polypeptide N-acetylgalactosaminyltransferase 17
- UniProt
- Q7TT15
- Pockets
- 1 · best druggability 0.73
Structure
1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polypeptide N-acetylgalactosaminyltransferase 17 | protein | 598 | 35% helix, 22% strand | Q7TT15 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 383 | 0.73 | 0.84 | 44 | empty |
Modifications
Observed in the structure: 5 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 Q7TT15
- Elsewhere: UniProt Q7TT15 · AlphaFold DB Q7TT15
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