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AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA helicase ruva (B2S1L2)
Analyse AlphaFold monomer V2.0 prediction for holliday junction ATP-dependent DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2S1L2
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x038799E20b082d1D917C74CF6645A0e30ad5a40e
- Molecule
- Holliday junction ATP-dependent DNA helicase ruva
- UniProt
- B2S1L2
- Pockets
- 1 · best druggability 0.64
Structure
1 distinct chain · 52% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction ATP-dependent DNA helicase ruva | protein | 196 | 52% helix, 20% strand | B2S1L2 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.64 | 0.87 | 21 | 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 B2S1L2
- Elsewhere: UniProt B2S1L2 · AlphaFold DB B2S1L2
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