Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A1B015)
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
- A1B015
- Type
- protein
- Length
- 1,382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7430138aDC76d97a0F1f6f3F14D160cC0dBf5ae6
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A1B015
- Pockets
- 18 · best druggability 0.82
Structure
1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1382 | 33% helix, 25% strand | A1B015 |
Pockets
18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 917 | 0.82 | 0.84 | 77 | empty |
| 2 | 937 | 0.75 | 0.79 | 109 | empty |
| 3 | 472 | 0.72 | 0.81 | 49 | empty |
| 4 | 230 | 0.63 | 0.82 | 27 | empty |
| 5 | 299 | 0.60 | 0.78 | 48 | 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 A1B015
- Elsewhere: UniProt A1B015 · AlphaFold DB A1B015
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