Research workbench
AlphaFold monomer V2.0 prediction for GDP-mannose 4,6-dehydratase sdni (A0A1B4XBH2)
Analyse AlphaFold monomer V2.0 prediction for GDP-mannose 4,6-dehydratase sdni… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A1B4XBH2
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3d944850D26fB5c0d71746C4caCa5CD27831DE39
- Molecule
- GDP-mannose 4,6-dehydratase sdni
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 28% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GDP-mannose 4,6-dehydratase sdni | protein | 544 | 28% helix, 17% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1192 | 0.78 | 0.80 | 102 | empty |
| 2 | 698 | 0.65 | 0.74 | 70 | empty |
| 3 | 61 | 0.28 | 0.73 | 14 | 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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