Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (Q5FKG6)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5FKG6
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- ATP-dependent 6-phosphofructokinase
- UniProt
- Q5FKG6
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase | protein | 320 | 47% helix, 21% strand | Q5FKG6 |
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 | 94 | 0.59 | 0.87 | 17 | empty |
| 2 | 153 | 0.46 | 0.77 | 27 | empty |
| 3 | 69 | 0.33 | 0.75 | 18 | 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 Q5FKG6
- Elsewhere: UniProt Q5FKG6 · AlphaFold DB Q5FKG6
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