Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (A1BD23)
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
- A1BD23
- Type
- protein
- Length
- 1,312 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- DNA-directed RNA polymerase subunit beta
- UniProt
- A1BD23
- Pockets
- 20 · best druggability 0.74
Structure
1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta | protein | 1312 | 33% helix, 25% strand | A1BD23 |
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 966 | 0.74 | 0.77 | 87 | empty |
| 2 | 519 | 0.66 | 0.77 | 50 | empty |
| 3 | 214 | 0.53 | 0.77 | 26 | empty |
| 4 | 175 | 0.51 | 0.78 | 24 | empty |
| 5 | 95 | 0.47 | 0.80 | 17 | 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 A1BD23
- Elsewhere: UniProt A1BD23 · AlphaFold DB A1BD23
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