Research workbench
AlphaFold monomer V2.0 prediction for undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase (Q0P9D0)
Analyse AlphaFold monomer V2.0 prediction for undecaprenyl phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0P9D0
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2b47CE81494c5321B3929F4cE4EA361c06Eba2E2
- Molecule
- Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
- UniProt
- Q0P9D0
- Pockets
- 2 · best druggability 0.73
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase | protein | 200 | 54% helix, 12% strand | Q0P9D0 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 601 | 0.73 | 0.81 | 43 | empty |
| 2 | 323 | 0.66 | 0.81 | 30 | 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 Q0P9D0
- Elsewhere: UniProt Q0P9D0 · AlphaFold DB Q0P9D0
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