Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (A4VHQ5)
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
- A4VHQ5
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- DNA-directed RNA polymerase subunit alpha
- UniProt
- A4VHQ5
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit alpha | protein | 333 | 29% helix, 30% strand | A4VHQ5 |
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 | 146 | 0.45 | 0.75 | 21 | empty |
| 2 | 55 | 0.37 | 0.80 | 20 | empty |
| 3 | 54 | 0.35 | 0.79 | 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 A4VHQ5
- Elsewhere: UniProt A4VHQ5 · AlphaFold DB A4VHQ5
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