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Crystal structure of fructokinase double-mutant (T261C-H108C) from vibrio cholerae O395 in fructose, ADP and potassium ion bound form

Analyse Crystal structure of fructokinase double-mutant (T261C-H108C) from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YGG
Type
protein
Length
310 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructokinase
EC
2.7.1.4
UniProt
A0A0H3AER7
Ligands
ADP, FRU, CA, K
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructokinase (EC 2.7.1.4)protein31042% helix, 23% strandA0A0H3AER7

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • FRU · beta-D-fructofuranose · sugar · chains A
  • CA · Calcium ion · metal · chains A
  • K · Potassium ion · metal · 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
14610.720.8261ADP, FRU, CA
2860.460.8114empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5YGG · Crystal structure of Fructokinase Double-Mutant (T261C-H108C) from Vibrio cholerae O395… · the same entry in another collection · chain A against A, TM-score 1.00

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