Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta'' (B1A925)
Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1A925
- Type
- protein
- Length
- 1,387 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x167C74E26f98Af17d629E9e0a9455d97c33EA927
- Molecule
- DNA-directed RNA polymerase subunit beta''
- UniProt
- B1A925
- Pockets
- 20 · best druggability 0.82
Structure
1 distinct chain · 24% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta'' | protein | 1387 | 24% helix, 21% strand | B1A925 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.82 | 0.83 | 114 | empty |
| 2 | 596 | 0.71 | 0.79 | 72 | empty |
| 3 | 806 | 0.68 | 0.75 | 70 | empty |
| 4 | 376 | 0.67 | 0.80 | 28 | empty |
| 5 | 751 | 0.66 | 0.74 | 53 | 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 B1A925
- Elsewhere: UniProt B1A925 · AlphaFold DB B1A925
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