Research workbench
AlphaFold monomer V2.0 prediction for probable copper-dependent oxygenase M1 (A0A3G1DJE8)
Analyse AlphaFold monomer V2.0 prediction for probable copper-dependent oxygenase M1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A3G1DJE8
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Probable copper-dependent oxygenase M1
- Pockets
- 2 · best druggability 0.63
Structure
1 distinct chain · 12% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable copper-dependent oxygenase M1 | protein | 386 | 12% helix, 42% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.63 | 0.83 | 43 | empty |
| 2 | 53 | 0.32 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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