Structure of PDB 3umo Chain A Binding Site BS01

Receptor Information
>3umo Chain A (length=309) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAH
LGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEAS
GEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLT
QLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELT
QPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQS
TVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDT
QKIYAYLSR
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain3umo Chain A Residue 313 [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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PDB3umo A Ribokinase Family Conserved Monovalent Cation Binding Site Enhances the MgATP-induced Inhibition in E. coli Phosphofructokinase-2
Resolution1.696 Å
Binding residue
(original residue number in PDB)		K185 N187 S224 G226 P227 G229 A254 G255 M258 V280 G283 S284 T287
Binding residue
(residue number reindexed from 1)		K185 N187 S224 G226 P227 G229 A254 G255 M258 V280 G283 S284 T287
Annotation score5
Binding affinityPDBbind-CN: -logKd/Ki=3.89,Ki=129uM
Enzymatic activity
Catalytic site (original residue number in PDB) G253 A254 G255 D256
Catalytic site (residue number reindexed from 1) G253 A254 G255 D256
Enzyme Commision number 2.7.1.11: 6-phosphofructokinase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003872 6-phosphofructokinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0009024 tagatose-6-phosphate kinase activity
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006096 glycolytic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0061615 glycolytic process through fructose-6-phosphate
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3umo, PDBe:3umo, PDBj:3umo
PDBsum3umo
PubMed23823238
UniProtP06999|PFKB_ECOLI ATP-dependent 6-phosphofructokinase isozyme 2 (Gene Name=pfkB)

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