Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (Q04E85)
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
- Q04E85
- Type
- protein
- Length
- 1,197 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71B2F470412030B8E2e004257dbF65C5d54BF3a8
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- Q04E85
- Pockets
- 20 · best druggability 0.70
Structure
1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1197 | 28% helix, 27% strand | Q04E85 |
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 490 | 0.70 | 0.80 | 60 | empty |
| 2 | 544 | 0.70 | 0.79 | 53 | empty |
| 3 | 52 | 0.64 | 0.95 | 17 | empty |
| 4 | 267 | 0.57 | 0.78 | 29 | empty |
| 5 | 95 | 0.49 | 0.81 | 25 | 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 Q04E85
- Elsewhere: UniProt Q04E85 · AlphaFold DB Q04E85
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