Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (A7HWT5)
Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7HWT5
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- DNA-directed RNA polymerase subunit alpha
- UniProt
- A7HWT5
- Pockets
- 3 · best druggability 0.49
Structure
1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit alpha | protein | 338 | 29% helix, 29% strand | A7HWT5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.49 | 0.75 | 23 | empty |
| 2 | 50 | 0.41 | 0.83 | 18 | empty |
| 3 | 54 | 0.30 | 0.76 | 12 | 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 A7HWT5
- Elsewhere: UniProt A7HWT5 · AlphaFold DB A7HWT5
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