Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (A9IVZ5)
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
- A9IVZ5
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF7cDBaE186D2224E9541810F108A2F47B9C78AD3
- Molecule
- DNA-directed RNA polymerase subunit alpha
- UniProt
- A9IVZ5
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit alpha | protein | 337 | 30% helix, 28% strand | A9IVZ5 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.52 | 0.76 | 27 | empty |
| 2 | 82 | 0.44 | 0.80 | 22 | empty |
| 3 | 88 | 0.35 | 0.75 | 18 | 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 A9IVZ5
- Elsewhere: UniProt A9IVZ5 · AlphaFold DB A9IVZ5
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