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Crystal structure of human ketohexokinase complexed to different sugar molecules

Analyse Crystal structure of human ketohexokinase complexed to different sugar molecules in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2HW1
Type
protein
Length
296 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ketohexokinase
EC
2.7.1.3
UniProt
P50053
Ligands
ANP, FRU, SO4
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKetohexokinase (EC 2.7.1.3)protein29637% helix, 24% strandP50053

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
  • FRU · beta-D-fructofuranose · sugar · chains A
  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15530.730.8155FRU, ANP

Compared structures

  • 2HW1 · Crystal structure of human ketohexokinase complexed to different sugar molecules · the same entry in another collection · chain A against A, TM-score 1.00
  • P50053 · AlphaFold monomer V2.0 prediction for ketohexokinase (P50053) · a predicted model of the same protein · chain A against A, TM-score 0.98

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