Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (B5ELX2)
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
- B5ELX2
- Type
- protein
- Length
- 1,362 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- B5ELX2
- Pockets
- 19 · best druggability 0.79
Structure
1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1362 | 33% helix, 25% strand | B5ELX2 |
Pockets
19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1037 | 0.79 | 0.80 | 86 | empty |
| 2 | 924 | 0.73 | 0.77 | 101 | empty |
| 3 | 51 | 0.66 | 0.96 | 17 | empty |
| 4 | 402 | 0.65 | 0.79 | 43 | empty |
| 5 | 122 | 0.51 | 0.81 | 26 | 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 B5ELX2
- Elsewhere: UniProt B5ELX2 · AlphaFold DB B5ELX2
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