Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A1E9I2)
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
- A1E9I2
- Type
- protein
- Length
- 682 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97C9199E55eA66e6305A49f17dB59c79b2766C48
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A1E9I2
- Pockets
- 7 · best druggability 0.70
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 682 | 42% helix, 16% strand | A1E9I2 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.70 | 0.93 | 18 | empty |
| 2 | 415 | 0.60 | 0.76 | 54 | empty |
| 3 | 355 | 0.58 | 0.76 | 37 | empty |
| 4 | 231 | 0.53 | 0.77 | 40 | empty |
| 5 | 100 | 0.41 | 0.77 | 19 | 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 A1E9I2
- Elsewhere: UniProt A1E9I2 · AlphaFold DB A1E9I2
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