Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A1D4V5)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase MPH1 (A1D4V5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1D4V5
- Type
- protein
- Length
- 1,111 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6b58efD144f1966f7848B5a8d2B96b73fc181639
- Molecule
- ATP-dependent DNA helicase MPH1
- UniProt
- A1D4V5
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 32% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase MPH1 | protein | 1111 | 32% helix, 7% strand | A1D4V5 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 932 | 0.76 | 0.79 | 103 | empty |
| 2 | 203 | 0.55 | 0.79 | 22 | empty |
| 3 | 137 | 0.40 | 0.74 | 21 | empty |
| 4 | 71 | 0.33 | 0.75 | 28 | empty |
| 5 | 61 | 0.32 | 0.75 | 16 | 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 A1D4V5
- Elsewhere: UniProt A1D4V5 · AlphaFold DB A1D4V5
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