Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (Q14FG5)
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
- Q14FG5
- Type
- protein
- Length
- 1,070 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4a9eD2eAf8d72EFA9810BAb10Ec13711141c1541
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- Q14FG5
- Pockets
- 17 · best druggability 0.69
Structure
1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1070 | 30% helix, 27% strand | Q14FG5 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 513 | 0.69 | 0.79 | 48 | empty |
| 2 | 54 | 0.68 | 0.97 | 20 | empty |
| 3 | 424 | 0.65 | 0.78 | 46 | empty |
| 4 | 449 | 0.59 | 0.74 | 55 | empty |
| 5 | 249 | 0.58 | 0.79 | 33 | 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 Q14FG5
- Elsewhere: UniProt Q14FG5 · AlphaFold DB Q14FG5
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