Research workbench
AlphaFold monomer V2.0 prediction for dolichyl- diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (E2R4X3)
Analyse AlphaFold monomer V2.0 prediction for dolichyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E2R4X3
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- UniProt
- E2R4X3
- Pockets
- 2 · best druggability 0.64
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 | protein | 119 | 75% helix, 0% strand | E2R4X3 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.64 | 0.77 | 41 | empty |
| 2 | 105 | 0.45 | 0.79 | 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 E2R4X3
- Elsewhere: UniProt E2R4X3 · AlphaFold DB E2R4X3
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