Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A3GH78)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A3GH78) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3GH78
- Type
- protein
- Length
- 1,050 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0B68cA60C95B982f45BEE070Fa9f83ABE55bc841
- Molecule
- ATP-dependent DNA helicase MPH1
- UniProt
- A3GH78
- Pockets
- 11 · best druggability 0.77
Structure
1 distinct chain · 36% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase MPH1 | protein | 1050 | 36% helix, 7% strand | A3GH78 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.77 | 0.85 | 56 | empty |
| 2 | 470 | 0.76 | 0.85 | 51 | empty |
| 3 | 249 | 0.70 | 0.85 | 30 | empty |
| 4 | 273 | 0.59 | 0.78 | 30 | empty |
| 5 | 84 | 0.49 | 0.83 | 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 A3GH78
- Elsewhere: UniProt A3GH78 · AlphaFold DB A3GH78
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