Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (B6EMS4)
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
- B6EMS4
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3f713B4B1650176e30B519F2A58Bd9E365E97fD0
- Molecule
- ATP-dependent 6-phosphofructokinase
- UniProt
- B6EMS4
- Pockets
- 2 · best druggability 0.49
Structure
1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase | protein | 320 | 46% helix, 20% strand | B6EMS4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.49 | 0.75 | 29 | empty |
| 2 | 51 | 0.33 | 0.78 | 13 | 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 B6EMS4
- Elsewhere: UniProt B6EMS4 · AlphaFold DB B6EMS4
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