Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A7HCH7)
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
- A7HCH7
- Type
- protein
- Length
- 1,416 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x08f1B0edc8474cb3B0f88330111598d367318E80
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A7HCH7
- Pockets
- 20 · best druggability 0.79
Structure
1 distinct chain · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1416 | 32% helix, 24% strand | A7HCH7 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1037 | 0.79 | 0.81 | 95 | empty |
| 2 | 606 | 0.71 | 0.79 | 56 | empty |
| 3 | 52 | 0.65 | 0.96 | 15 | empty |
| 4 | 486 | 0.64 | 0.77 | 48 | empty |
| 5 | 271 | 0.63 | 0.80 | 41 | 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 A7HCH7
- Elsewhere: UniProt A7HCH7 · AlphaFold DB A7HCH7
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