Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A5IHS0)
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
- A5IHS0
- Type
- protein
- Length
- 1,401 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A5IHS0
- Pockets
- 17 · best druggability 0.81
Structure
1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1401 | 40% helix, 19% strand | A5IHS0 |
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.81 | 0.82 | 80 | empty |
| 2 | 933 | 0.76 | 0.79 | 75 | empty |
| 3 | 884 | 0.70 | 0.75 | 52 | empty |
| 4 | 644 | 0.70 | 0.77 | 39 | empty |
| 5 | 624 | 0.67 | 0.77 | 46 | 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 A5IHS0
- Elsewhere: UniProt A5IHS0 · AlphaFold DB A5IHS0
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