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Crystal structure of fructokinase with ADP and fructose bound in the active site

Analyse Crystal structure of fructokinase with ADP and fructose bound in the active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LM9
Type
protein
Length
294 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructokinase
EC
2.7.1.4
UniProt
O05510
Ligands
ADP, FRU, ZN, SO4
Pockets
2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructokinase (EC 2.7.1.4)protein29440% helix, 20% strandO05510

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • FRU · beta-D-fructofuranose · sugar · chains A
  • ZN · Zinc ion · metal · chains A
  • SO4 · Sulfate 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15770.680.7860FRU
21290.450.7722empty

Modifications

Observed in the structure: 8 modified (engineered, methylation).

Compared structures

  • 3LM9 · Crystal structure of fructokinase with ADP and Fructose bound in the active site · the same entry in another collection · chain A against A, TM-score 1.00
  • O05510 · AlphaFold monomer V2.0 prediction for putative fructokinase (O05510) · a predicted model of the same protein · chain A against A, TM-score 0.99

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