Structure of PDB 6sy7 Chain D Binding Site BS01

Receptor Information
>6sy7 Chain D (length=452) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NSVTQEDLKVDRLPGADYPNPSKKYSSRTEFRDKTDYIMYNPRPRDEPSS
ENPVSVSPLLCELAAARSRIHFNPTETTIGIVTCGGICPGLNDVIRSITL
TGINVYNVKRVIGFRFGYWGLSKKGSQTAIELHRGRVTNIHHYGGTILGS
SRGPQDPKEMVDTLERLGVNILFTVGGDGTQRGALVISQEAKRRGVDISV
FGVPKTIDNDLSFSHRTFGFQTAVEKAVQAIRAAYAEAVSANYGVGVVKL
MGRDSGFIAAQAAVASAQANICLVPENPISEQEVMSLLERRFCHSRSCVI
IVAEGFGQDWGIDIGVILTEKVKAFLKANKSRYPDSTVKYIDPSYMIRAC
PPSANDALFCATLATLAVHEAMAGATGCIIAMRHNNYILVPIKVATSVRR
VLDLRGQLWRQVREITVDLGSDVRLARKLEIRRELEAINRNRDRLHEELA
KL
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain6sy7 Chain C Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6sy7 Kinetic and structural studies of Trypanosoma and Leishmania phosphofructokinases show evolutionary divergence and identify AMP as a switch regulating glycolysis versus gluconeogenesis.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		R117 S118 L121 N125 R155
Binding residue
(residue number reindexed from 1)		R96 S97 L100 N104 R134
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G107 R173 G174 D199 G200 K226 T227 D229 D231 R274
Catalytic site (residue number reindexed from 1) G86 R152 G153 D178 G179 K205 T206 D208 D210 R253
Enzyme Commision number 2.7.1.11: 6-phosphofructokinase.
Gene Ontology
Molecular Function
GO:0003872 6-phosphofructokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042301 phosphate ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
GO:0061615 glycolytic process through fructose-6-phosphate
Cellular Component
GO:0005737 cytoplasm
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6sy7, PDBe:6sy7, PDBj:6sy7
PDBsum6sy7
PubMed31838765
UniProtO15648|PFKA_TRYBB ATP-dependent 6-phosphofructokinase (Gene Name=pfk)

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