Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A4XI30)
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
- A4XI30
- Type
- protein
- Length
- 1,229 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDdA5c544dDF868DE45EbEc3719D1dBE78eEBaD3B
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A4XI30
- Pockets
- 18 · best druggability 0.74
Structure
1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1229 | 30% helix, 26% strand | A4XI30 |
Pockets
18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 626 | 0.74 | 0.81 | 61 | empty |
| 2 | 670 | 0.74 | 0.80 | 74 | empty |
| 3 | 984 | 0.72 | 0.76 | 77 | empty |
| 4 | 872 | 0.70 | 0.76 | 56 | empty |
| 5 | 58 | 0.69 | 0.97 | 16 | 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 A4XI30
- Elsewhere: UniProt A4XI30 · AlphaFold DB A4XI30
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