Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase II subunit 1 (Q2H0I3)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase II subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2H0I3
- Type
- protein
- Length
- 622 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- ATP-dependent DNA helicase II subunit 1
- UniProt
- Q2H0I3
- Pockets
- 8 · best druggability 0.77
Structure
1 distinct chain · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase II subunit 1 | protein | 622 | 34% helix, 16% strand | Q2H0I3 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.77 | 0.79 | 86 | empty |
| 2 | 795 | 0.75 | 0.79 | 65 | empty |
| 3 | 183 | 0.47 | 0.75 | 28 | empty |
| 4 | 178 | 0.45 | 0.74 | 23 | empty |
| 5 | 119 | 0.44 | 0.77 | 24 | 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 Q2H0I3
- Elsewhere: UniProt Q2H0I3 · AlphaFold DB Q2H0I3
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