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Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate

Analyse Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ALD
Type
protein
Length
363 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-bisphosphate aldolase
EC
4.1.2.13
UniProt
P04075
Ligands
2FP
Pockets
3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructose-bisphosphate aldolase (EC 4.1.2.13)protein36344% helix, 15% strandP04075

Ligands and binding sites

  • 2FP · 1,6-fructose diphosphate (linear form) · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15730.770.84472FP
21260.490.8022empty
3590.340.7816empty

Compared structures

  • 4ALD · Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate · the same entry in another collection · chain A against A, TM-score 1.00
  • P04075 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P04075) · a predicted model of the same protein · chain A against A, TM-score 0.99

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