Structure of PDB 5xvu Chain A Binding Site BS01

Receptor Information
>5xvu Chain A (length=321) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IPKFYADVNIHKPKEYYDYDNLELQWNKPNRYEIMKKIGRGKYSEVFNGY
DTECNRPCAIKVLKPVKKKKIKREIKILQNLNGGPNIIKLLDIVKDPVTK
TPSLIFEYINNIDFKTLYPKFTDKDIRYYIYQILKALDYCHSQGIMHRDV
KPHNIMIDHENRQIRLISWGLAEFYHPGQEYNVRVASRYYKGPELLIDLQ
LYDYSLDIWSLGCMLAGMIFKKEPFFCGHDNYDQLVKIAKVLGTEDLHAY
LKKYNIKLKPHYLNILGEYERKPWSHFLTQSNIDIAKDEVIDLIDKMLIY
DHAKRIAPKEAMEHPYFREVR
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 chain5xvu Chain A Residue 403 [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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PDB5xvu The protein kinase CK2 catalytic domain from Plasmodium falciparum: crystal structure, tyrosine kinase activity and inhibition.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		G50 K53 Y54 S55 V57 A70 K72 I120 M167 I178 S179
Binding residue
(residue number reindexed from 1)		G39 K42 Y43 S44 V46 A59 K61 I109 M156 I167 S168
Annotation score5
Binding affinityPDBbind-CN: -logKd/Ki=4.65,Kd=22.3uM
Enzymatic activity
Catalytic site (original residue number in PDB) D160 K162 N165 S179 S198
Catalytic site (residue number reindexed from 1) D149 K151 N154 S168 S187
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
GO:0019901 protein kinase binding
GO:0044024 histone H2AS1 kinase activity
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0046777 protein autophosphorylation
GO:0051726 regulation of cell cycle
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005956 protein kinase CK2 complex
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5xvu, PDBe:5xvu, PDBj:5xvu
PDBsum5xvu
PubMed29743645
UniProtQ8IIR9

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