Research workbench
AlphaFold monomer V2.0 prediction for glycosyltransferase-like protein GNT15 (Q555X4)
Analyse AlphaFold monomer V2.0 prediction for glycosyltransferase-like protein GNT15… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q555X4
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1a68bc8B8a369482B790efFfC148F4639Ac79877
- Molecule
- Glycosyltransferase-like protein GNT15
- UniProt
- Q555X4
- Pockets
- 7 · best druggability 0.71
Structure
1 distinct chain · 35% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyltransferase-like protein GNT15 | protein | 516 | 35% helix, 12% strand | Q555X4 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.71 | 0.81 | 49 | empty |
| 2 | 253 | 0.54 | 0.77 | 23 | empty |
| 3 | 98 | 0.54 | 0.84 | 24 | empty |
| 4 | 134 | 0.47 | 0.78 | 19 | empty |
| 5 | 166 | 0.45 | 0.75 | 26 | empty |
Modifications
Observed in the structure: 2 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 Q555X4
- Elsewhere: UniProt Q555X4 · AlphaFold DB Q555X4
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