Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (P21421)
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
- P21421
- Type
- protein
- Length
- 1,024 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD904A62Eecaad31A1EEd697d993525ba9E3f643b
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- P21421
- Pockets
- 20 · best druggability 0.65
Structure
1 distinct chain · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1024 | 28% helix, 28% strand | P21421 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.65 | 0.82 | 33 | empty |
| 2 | 536 | 0.63 | 0.74 | 43 | empty |
| 3 | 402 | 0.63 | 0.78 | 42 | empty |
| 4 | 401 | 0.63 | 0.77 | 55 | empty |
| 5 | 126 | 0.61 | 0.85 | 20 | 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 P21421
- Elsewhere: UniProt P21421 · AlphaFold DB P21421
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