Research workbench
PFKFB3 in complex with ADP and pep
Analyse PFKFB3 in complex with ADP and pep in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DWO
- 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
- F6P, ADP, PEP
- 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 |
|---|---|---|---|---|---|
| A | 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
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- PEP · Phosphoenolpyruvate · ligand · 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 | 629 | 0.82 | 0.87 | 87 | ADP, PEP |
| 2 | 225 | 0.77 | 0.91 | 41 | F6P |
Compared structures
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 2DWO · PDBe 2DWO · UniProt Q16875
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