Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized ATP-binding protein MJ1609 (Q59004)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q59004
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Uncharacterized ATP-binding protein MJ1609
- UniProt
- Q59004
- Pockets
- 4 · best druggability 0.51
Structure
1 distinct chain · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized ATP-binding protein MJ1609 | protein | 374 | 55% helix, 16% strand | Q59004 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.51 | 0.80 | 24 | empty |
| 2 | 168 | 0.48 | 0.76 | 20 | empty |
| 3 | 113 | 0.38 | 0.75 | 23 | empty |
| 4 | 99 | 0.36 | 0.74 | 21 | 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 Q59004
- Elsewhere: UniProt Q59004 · AlphaFold DB Q59004
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