Research workbench
PFKFB3 in complex with Aluminum Tetrafluoride
Analyse PFKFB3 in complex with Aluminum Tetrafluoride in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QPW
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- Homo sapiens
- Molecule
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- EC
- 2.7.1.105, 3.1.3.46
- UniProt
- Q16875
- Ligands
- ALF, ADP, PEP, CL
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · resolution 2.25 · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (EC 2.7.1.105, 3.1.3.46) | protein | 431 | 44% helix, 18% strand | Q16875 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- PEP · Phosphoenolpyruvate · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 613 | 0.83 | 0.88 | 77 | ADP, PEP, CL |
| 2 | 259 | 0.64 | 0.82 | 41 | ALF |
Compared structures
- 3QPW · PFKFB3 in complex with aluminum tetrafluoride · the same entry in another collection · chain A against A, TM-score 1.00
- Q16875 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q16875
- Elsewhere: RCSB PDB 3QPW · PDBe 3QPW · UniProt Q16875
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