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Human PFKFB3 in complex with KAN0438241

Analyse Human PFKFB3 in complex with KAN0438241 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ETJ
Type
protein
Length
432 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase 3
EC
2.7.1.105, 3.1.3.46
UniProt
Q16875
Ligands
F6P, BWW, ADP
Pockets
2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase 3 (EC 2.7.1.105, 3.1.3.46)protein43244% helix, 18% strandQ16875

Ligands and binding sites

  • F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
  • BWW · 4-[[3-(5-fluoranyl-2-oxidanyl-phenyl) phenyl]sulfonylamino]-2-oxidanyl-benzoic acid · ligand · chains A
  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • DMS · Dimethyl sulfoxide · additive · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16480.820.8681BWW, ADP
22180.710.8846F6P

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 6ETJ · Human PFKFB3 in complex with KAN0438241 · 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

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