Structure of PDB 3ump Chain B Binding Site BS01

Receptor Information
>3ump Chain B (length=308) 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
QKIYAYLS
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 chain3ump Chain B Residue 312 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ump A Ribokinase Family Conserved Monovalent Cation Binding Site Enhances the MgATP-induced Inhibition in E. coli Phosphofructokinase-2
Resolution1.849 Å
Binding residue
(original residue number in PDB)		Y23 G26 K27
Binding residue
(residue number reindexed from 1)		Y23 G26 K27
Annotation score5
Binding affinityPDBbind-CN: -logKd/Ki=2.99,Ki=1026uM
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:3ump, PDBe:3ump, PDBj:3ump
PDBsum3ump
PubMed23823238
UniProtP06999|PFKB_ECOLI ATP-dependent 6-phosphofructokinase isozyme 2 (Gene Name=pfkB)

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