Structure of PDB 4rlk Chain A

Receptor sequence
>4rlkA (length=327) Species: 4577 (Zea mays) [Search protein sequence]
SKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEG
INVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQHS
KTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHRD
VKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDL
QDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLNV
YLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLLR
YDHQERLTALEAMTHPYFQQVRAAENS
3D structure
PDB4rlk Protein kinase CK2 inhibition is associated with the destabilization of HIF-1 alpha in human cancer cells.
ChainA
Resolution1.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D156 K158 N161 D175 S194
Catalytic site (residue number reindexed from 1) D150 K152 N155 D169 S188
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 E91 A V45 I66 K68 V95 F113 Y115 V116 N118 M163 I174 D175 V39 I60 K62 V89 F107 Y109 V110 N112 M157 I168 D169 PDBbind-CN: -logKd/Ki=5.02,IC50=9.5uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP 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:0051726 regulation of cell cycle
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol
GO:0005956 protein kinase CK2 complex
GO:0043231 intracellular membrane-bounded organelle

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Cellular Component
External links
PDB RCSB:4rlk, PDBe:4rlk, PDBj:4rlk
PDBsum4rlk
PubMed25449433
UniProtP28523|CSK2A_MAIZE Casein kinase II subunit alpha (Gene Name=ACK2)

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