Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A2SLG5)
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
- A2SLG5
- Type
- protein
- Length
- 1,375 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAB101f7Cfd0D22Bf85F642916550b92ff64174f9
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A2SLG5
- Pockets
- 14 · best druggability 0.81
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1375 | 34% helix, 25% strand | A2SLG5 |
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.81 | 0.83 | 90 | empty |
| 2 | 940 | 0.73 | 0.77 | 96 | empty |
| 3 | 59 | 0.69 | 0.96 | 21 | empty |
| 4 | 443 | 0.68 | 0.80 | 49 | empty |
| 5 | 154 | 0.50 | 0.78 | 24 | 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 A2SLG5
- Elsewhere: UniProt A2SLG5 · AlphaFold DB A2SLG5
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