Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (Q5HDY4)
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
- Q5HDY4
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- DNA-directed RNA polymerase subunit alpha
- UniProt
- Q5HDY4
- Pockets
- 3 · best druggability 0.47
Structure
1 distinct chain · 29% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit alpha | protein | 314 | 29% helix, 33% strand | Q5HDY4 |
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 | 0.47 | 0.76 | 23 | empty |
| 2 | 56 | 0.42 | 0.82 | 21 | empty |
| 3 | 51 | 0.28 | 0.75 | 11 | 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 Q5HDY4
- Elsewhere: UniProt Q5HDY4 · AlphaFold DB Q5HDY4
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