Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A1XFU6)
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
- A1XFU6
- Type
- protein
- Length
- 693 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A1XFU6
- Pockets
- 9 · best druggability 0.72
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 693 | 40% helix, 15% strand | A1XFU6 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 674 | 0.72 | 0.78 | 61 | empty |
| 2 | 476 | 0.66 | 0.78 | 44 | empty |
| 3 | 421 | 0.60 | 0.75 | 43 | empty |
| 4 | 63 | 0.41 | 0.81 | 15 | empty |
| 5 | 50 | 0.34 | 0.78 | 13 | 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 A1XFU6
- Elsewhere: UniProt A1XFU6 · AlphaFold DB A1XFU6
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