Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A3P0C5)
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
- A3P0C5
- Type
- protein
- Length
- 1,368 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A3P0C5
- Pockets
- 14 · best druggability 0.78
Structure
1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1368 | 33% helix, 24% strand | A3P0C5 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1036 | 0.78 | 0.80 | 83 | empty |
| 2 | 569 | 0.75 | 0.82 | 52 | empty |
| 3 | 521 | 0.70 | 0.80 | 51 | empty |
| 4 | 365 | 0.58 | 0.76 | 56 | empty |
| 5 | 182 | 0.51 | 0.78 | 34 | 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 A3P0C5
- Elsewhere: UniProt A3P0C5 · AlphaFold DB A3P0C5
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