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Crystal structure of the complex of phosphofructokinase from escherichia COLI with its reaction products

Analyse Crystal structure of the complex of phosphofructokinase from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PFK
Type
protein
Length
640 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphofructokinase
EC
2.7.1.11
UniProt
P0A796
Ligands
ADP, FBP, MG
Pockets
10 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhosphofructokinase (EC 2.7.1.11)protein32047% helix, 19% strandP0A796

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B
  • FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.660.8432empty
21490.620.8531empty
32220.560.7933FBP, MG, ADP
42600.550.7734FBP, ADP
52340.530.7631empty

Interfaces

1 interface between chains.

  • A–B · 1964 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 1PFK · Crystal structure of the complex of phosphofructokinase from escherichia COLI with its… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A796 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase isozyme 1… · a predicted model of the same protein · chain A against A, TM-score 0.99

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