Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A1BD24)
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
- A1BD24
- Type
- protein
- Length
- 1,492 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A1BD24
- Pockets
- 20 · best druggability 0.80
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1492 | 38% helix, 18% strand | A1BD24 |
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 | 975 | 0.80 | 0.81 | 64 | empty |
| 2 | 672 | 0.73 | 0.80 | 69 | empty |
| 3 | 605 | 0.73 | 0.80 | 56 | empty |
| 4 | 1011 | 0.71 | 0.75 | 66 | empty |
| 5 | 527 | 0.71 | 0.80 | 63 | 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 A1BD24
- Elsewhere: UniProt A1BD24 · AlphaFold DB A1BD24
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