Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (Q30X05)
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
- Q30X05
- Type
- protein
- Length
- 1,375 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- Q30X05
- Pockets
- 15 · best druggability 0.81
Structure
1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1375 | 32% helix, 25% strand | Q30X05 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1034 | 0.81 | 0.82 | 79 | empty |
| 2 | 798 | 0.73 | 0.78 | 78 | empty |
| 3 | 377 | 0.61 | 0.77 | 43 | empty |
| 4 | 281 | 0.58 | 0.78 | 31 | empty |
| 5 | 274 | 0.57 | 0.77 | 45 | 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 Q30X05
- Elsewhere: UniProt Q30X05 · AlphaFold DB Q30X05
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