Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A7EFH4)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A7EFH4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7EFH4
- Type
- protein
- Length
- 1,235 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x431CFe1eAbd5D5954346E0071B3917b9D0600749
- Molecule
- ATP-dependent DNA helicase MPH1
- UniProt
- A7EFH4
- Pockets
- 7 · best druggability 0.82
Structure
1 distinct chain · 27% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase MPH1 | protein | 1235 | 27% helix, 6% strand | A7EFH4 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.82 | 0.84 | 111 | empty |
| 2 | 237 | 0.58 | 0.79 | 31 | empty |
| 3 | 122 | 0.43 | 0.76 | 17 | empty |
| 4 | 116 | 0.42 | 0.77 | 26 | empty |
| 5 | 104 | 0.40 | 0.76 | 26 | 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 A7EFH4
- Elsewhere: UniProt A7EFH4 · AlphaFold DB A7EFH4
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