Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A1TVT0)
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
- A1TVT0
- Type
- protein
- Length
- 1,374 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A1TVT0
- Pockets
- 13 · best druggability 0.77
Structure
1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1374 | 33% helix, 25% strand | A1TVT0 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1174 | 0.77 | 0.79 | 93 | empty |
| 2 | 573 | 0.72 | 0.80 | 53 | empty |
| 3 | 471 | 0.70 | 0.80 | 42 | empty |
| 4 | 478 | 0.61 | 0.75 | 70 | empty |
| 5 | 323 | 0.57 | 0.76 | 46 | 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 A1TVT0
- Elsewhere: UniProt A1TVT0 · AlphaFold DB A1TVT0
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