Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (P0DF31)
Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DF31
- Type
- protein
- Length
- 1,188 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE63d721Ad9B1660e8d03c7C92c3F8d8349400985
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- P0DF31
- Pockets
- 20 · best druggability 0.70
Structure
1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1188 | 29% helix, 27% strand | P0DF31 |
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 382 | 0.70 | 0.83 | 35 | empty |
| 2 | 560 | 0.68 | 0.78 | 53 | empty |
| 3 | 529 | 0.67 | 0.78 | 45 | empty |
| 4 | 56 | 0.67 | 0.96 | 17 | empty |
| 5 | 234 | 0.54 | 0.77 | 34 | 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 P0DF31
- Elsewhere: UniProt P0DF31 · AlphaFold DB P0DF31
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