Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (Q5PBG3)
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
- Q5PBG3
- Type
- protein
- Length
- 1,415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x170c3D99552C36Afe2B5B1367e2Af517d767f104
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- Q5PBG3
- Pockets
- 18 · best druggability 0.78
Structure
1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1415 | 40% helix, 19% strand | Q5PBG3 |
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 646 | 0.78 | 0.84 | 53 | empty |
| 2 | 1185 | 0.78 | 0.80 | 105 | empty |
| 3 | 811 | 0.71 | 0.77 | 77 | empty |
| 4 | 901 | 0.69 | 0.74 | 60 | empty |
| 5 | 592 | 0.68 | 0.76 | 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 Q5PBG3
- Elsewhere: UniProt Q5PBG3 · AlphaFold DB Q5PBG3
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