Research workbench
AlphaFold monomer V2.0 prediction for er-bound oxygenase mpab' (A0A0B5LB52)
Analyse AlphaFold monomer V2.0 prediction for er-bound oxygenase mpab' (A0A0B5LB52) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A0B5LB52
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29EAdEfF44bDA42f96B33481D606dd403a9e4547
- Molecule
- Er-bound oxygenase mpab'
- Pockets
- 4 · best druggability 0.85
Structure
1 distinct chain · 65% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Er-bound oxygenase mpab' | protein | 423 | 65% helix, 1% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.85 | 0.94 | 39 | empty |
| 2 | 225 | 0.78 | 0.92 | 34 | empty |
| 3 | 387 | 0.70 | 0.81 | 37 | empty |
| 4 | 51 | 0.30 | 0.76 | 11 | 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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