Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (B5EFP4)
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
- B5EFP4
- Type
- protein
- Length
- 1,382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- B5EFP4
- Pockets
- 20 · best druggability 0.77
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1382 | 39% helix, 20% strand | B5EFP4 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.77 | 0.82 | 58 | empty |
| 2 | 376 | 0.75 | 0.86 | 41 | empty |
| 3 | 647 | 0.71 | 0.78 | 46 | empty |
| 4 | 645 | 0.70 | 0.78 | 42 | empty |
| 5 | 900 | 0.70 | 0.75 | 52 | 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 B5EFP4
- Elsewhere: UniProt B5EFP4 · AlphaFold DB B5EFP4
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