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Structure of trypanosome brucei phosphofructokinase in complex with AMP.

Analyse Structure of trypanosome brucei phosphofructokinase in complex with AMP. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SY7
Type
protein
Length
3,618 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
O15648
Ligands
BNZ, AMP

Structure

x-ray diffraction · 8 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein455—O15648
B—protein454—O15648
C—protein451—O15648
D—protein452—O15648
E—protein450—O15648
F—protein450—O15648
G—protein452—O15648
H—protein454—O15648

Ligands and binding sites

  • BNZ · Benzene · ligand · 8 copies · chains A, B, C, D, E, F, G, H
  • AMP · Adenosine monophosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
  • GOL · Glycerol · additive · 8 copies · chains A, B, C, D, E, F, G, H

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

Compared structures

  • 6SY7 · Structure of Trypanosome Brucei Phosphofructokinase in complex with AMP. · the same entry in another collection · chain H against H, TM-score 1.00
  • O15648 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (O15648) · a predicted model of the same protein · chain E against A, TM-score 0.93

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