Research workbench
AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase ptmm (A0A140JWT1)
Analyse AlphaFold monomer V2.0 prediction for FAD-dependent monooxygenase ptmm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A140JWT1
- Type
- protein
- Length
- 422 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x58f6e67D5142B70031Af746651e7a6442367610c
- Molecule
- FAD-dependent monooxygenase ptmm
- Pockets
- 2 · best druggability 0.83
Structure
1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-dependent monooxygenase ptmm | protein | 422 | 41% helix, 27% 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 | 978 | 0.83 | 0.84 | 93 | empty |
| 2 | 75 | 0.33 | 0.75 | 21 | empty |
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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