Research workbench
AlphaFold monomer V2.0 prediction for beta-1,2-xylosyltransferase (Q9LDH0)
Analyse AlphaFold monomer V2.0 prediction for beta-1,2-xylosyltransferase (Q9LDH0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LDH0
- Type
- protein
- Length
- 534 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0077fc365c9e89D7eb2784e55eCD39C0bedB05a1
- Molecule
- Beta-1,2-xylosyltransferase
- UniProt
- Q9LDH0
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 31% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1,2-xylosyltransferase | protein | 534 | 31% helix, 18% strand | Q9LDH0 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 797 | 0.73 | 0.78 | 87 | empty |
| 2 | 145 | 0.51 | 0.79 | 19 | empty |
| 3 | 98 | 0.41 | 0.78 | 23 | empty |
| 4 | 53 | 0.32 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 4 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 Q9LDH0
- Elsewhere: UniProt Q9LDH0 · AlphaFold DB Q9LDH0
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