Research workbench
AlphaFold monomer V2.0 prediction for N-acetylglucosaminyl-diphospho- decaprenol L-rhamnosyltransferase (P9WMY2)
Analyse AlphaFold monomer V2.0 prediction for N-acetylglucosaminyl-diphospho… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P9WMY2
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
- UniProt
- P9WMY2
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase | protein | 307 | 45% helix, 21% strand | P9WMY2 |
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 | 577 | 0.76 | 0.83 | 54 | empty |
| 2 | 101 | 0.42 | 0.77 | 17 | 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 P9WMY2
- Elsewhere: UniProt P9WMY2 · AlphaFold DB P9WMY2
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