Research workbench
AlphaFold monomer V2.0 prediction for O-antigen polymerase (P0A236)
Analyse AlphaFold monomer V2.0 prediction for O-antigen polymerase (P0A236) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A236
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- O-antigen polymerase
- UniProt
- P0A236
- Pockets
- 6 · best druggability 0.79
Structure
1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-antigen polymerase | protein | 407 | 69% helix, 0% strand | P0A236 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.79 | 0.85 | 47 | empty |
| 2 | 261 | 0.67 | 0.83 | 36 | empty |
| 3 | 176 | 0.61 | 0.82 | 23 | empty |
| 4 | 311 | 0.57 | 0.76 | 28 | empty |
| 5 | 53 | 0.38 | 0.79 | 11 | 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 P0A236
- Elsewhere: UniProt P0A236 · AlphaFold DB P0A236
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