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Fructose-1,6-bisphosphatase complex with AMP, zinc, fructose-6- phosphate and phosphate (T-state)

Analyse Fructose-1,6-bisphosphatase complex with AMP, zinc, fructose-6- phosphate and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EYK
Type
protein
Length
654 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-1,6-bisphosphatase
EC
3.1.3.11
UniProt
P00636
Ligands
F6P, AMP, ZN, PO4
Pockets
9 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFructose-1,6-bisphosphatase (EC 3.1.3.11)protein32736% helix, 24% strandP00636

Ligands and binding sites

  • F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
  • AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13570.610.7734empty
21600.540.8135F6P, PO4
31560.530.8038F6P, PO4
41580.510.7823empty
51190.460.7818empty

Interfaces

1 interface between chains.

  • A–B · 2428 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 1EYK · Fructose-1,6-bisphosphatase complex with AMP, zinc, fructose-6-phosphate and phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain A against A, TM-score 0.95

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