Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (Q8VU09)
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
- Q8VU09
- Type
- protein
- Length
- 459 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x66026B7eDA2C7707c7042FCF1BE7d1A483c4dD3c
- Molecule
- ATP-dependent 6-phosphofructokinase
- UniProt
- Q8VU09
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase | protein | 459 | 37% helix, 17% strand | Q8VU09 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.73 | 0.82 | 56 | empty |
| 2 | 289 | 0.54 | 0.76 | 25 | empty |
| 3 | 159 | 0.48 | 0.77 | 23 | empty |
| 4 | 78 | 0.30 | 0.72 | 16 | 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 Q8VU09
- Elsewhere: UniProt Q8VU09 · AlphaFold DB Q8VU09
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