Research workbench
AlphaFold monomer V2.0 prediction for O-antigen biosynthesis protein rfbc (Q50864)
Analyse AlphaFold monomer V2.0 prediction for O-antigen biosynthesis protein rfbc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q50864
- Type
- protein
- Length
- 1,275 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x079259f5Fd4eeDe65D1d953dAFA16Bf9e3204575
- Molecule
- O-antigen biosynthesis protein rfbc
- UniProt
- Q50864
- Pockets
- 8 · best druggability 0.77
Structure
1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-antigen biosynthesis protein rfbc | protein | 1275 | 47% helix, 16% strand | Q50864 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 807 | 0.77 | 0.81 | 71 | empty |
| 2 | 760 | 0.77 | 0.81 | 62 | empty |
| 3 | 707 | 0.74 | 0.80 | 68 | empty |
| 4 | 295 | 0.55 | 0.76 | 28 | empty |
| 5 | 274 | 0.53 | 0.75 | 53 | 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 Q50864
- Elsewhere: UniProt Q50864 · AlphaFold DB Q50864
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