Research workbench
Crystal structure of PFKFB3 in complex with ADP and fructose-2,6- bisphosphate
Analyse Crystal structure of PFKFB3 in complex with ADP and fructose-2,6- bisphosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I1V
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 3
- EC
- 2.7.1.105, 3.1.3.46
- UniProt
- Q16875
- Ligands
- FDP, F6P, ADP, PHS
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 3 (EC 2.7.1.105, 3.1.3.46) | protein | 449 | 43% helix, 17% strand | Q16875 |
Ligands and binding sites
- FDP · 2,6-di-O-phosphono-beta-D-fructofuranose · ligand · chains B
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains B
- ADP · Adenosine-5'-diphosphate · ligand · chains B
- PHS · Phosphonic acid · ligand · chains B
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 | 682 | 0.82 | 0.86 | 85 | FDP, ADP |
| 2 | 239 | 0.77 | 0.91 | 44 | F6P, PHS |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2I1V · Crystal structure of PFKFB3 in complex with ADP and Fructose-2,6-bisphosphate · the same entry in another collection · chain B against B, 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 B against A, TM-score 0.98
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 2I1V · PDBe 2I1V · UniProt Q16875
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