Research workbench
AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1 (A4SWM3)
Analyse AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4SWM3
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x917B68ac5F3261871D3Df8D41b8Dd121B8830247
- Molecule
- Fructose-1,6-bisphosphatase class 1
- UniProt
- A4SWM3
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase class 1 | protein | 335 | 36% helix, 26% strand | A4SWM3 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.61 | 0.84 | 26 | empty |
| 2 | 72 | 0.37 | 0.78 | 21 | empty |
| 3 | 62 | 0.29 | 0.74 | 14 | 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 A4SWM3
- Elsewhere: UniProt A4SWM3 · AlphaFold DB A4SWM3
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