Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized glycosyltransferase SLL0501 (Q55487)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized glycosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q55487
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Uncharacterized glycosyltransferase SLL0501
- UniProt
- Q55487
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized glycosyltransferase SLL0501 | protein | 318 | 52% helix, 15% strand | Q55487 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 933 | 0.76 | 0.79 | 79 | empty |
| 2 | 166 | 0.56 | 0.81 | 17 | empty |
| 3 | 67 | 0.36 | 0.77 | 13 | empty |
Compared structures
- 5EKP · Structure of the polyisoprenyl-phosphate glycosyltransferase gtrb (wt) · an experimental structure of the same protein · chain A against C, TM-score 0.83
- 5EKP · Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) · an experimental structure of the same protein · chain A against C, TM-score 0.83
- 5EKE · Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) · an experimental structure of the same protein · chain A against C, TM-score 0.83
- 5EKE · Structure of the polyisoprenyl-phosphate glycosyltransferase gtrb (F215A mutant) · an experimental structure of the same protein · chain A against C, TM-score 0.83
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 Q55487
- Elsewhere: UniProt Q55487 · AlphaFold DB Q55487
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