Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A4TS28)
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
- A4TS28
- Type
- protein
- Length
- 1,406 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A4TS28
- Pockets
- 19 · best druggability 0.78
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1406 | 39% helix, 20% strand | A4TS28 |
Pockets
19 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1193 | 0.78 | 0.80 | 84 | empty |
| 2 | 727 | 0.75 | 0.80 | 56 | empty |
| 3 | 946 | 0.71 | 0.76 | 57 | empty |
| 4 | 760 | 0.71 | 0.77 | 72 | empty |
| 5 | 591 | 0.69 | 0.77 | 39 | 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 A4TS28
- Elsewhere: UniProt A4TS28 · AlphaFold DB A4TS28
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