Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase II subunit 1 (Q2MHH3)
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
- Q2MHH3
- Type
- protein
- Length
- 655 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- ATP-dependent DNA helicase II subunit 1
- UniProt
- Q2MHH3
- Pockets
- 6 · best druggability 0.82
Structure
1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase II subunit 1 | protein | 655 | 35% helix, 19% strand | Q2MHH3 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.82 | 0.83 | 117 | empty |
| 2 | 58 | 0.40 | 0.81 | 12 | empty |
| 3 | 128 | 0.39 | 0.73 | 15 | empty |
| 4 | 67 | 0.37 | 0.78 | 17 | empty |
| 5 | 84 | 0.35 | 0.76 | 18 | 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 Q2MHH3
- Elsewhere: UniProt Q2MHH3 · AlphaFold DB Q2MHH3
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