Structure of PDB 1m2p Chain A

Receptor sequence
>1m2pA (length=325) Species: 4577 (Zea mays) [Search protein sequence]
SKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEG
INVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQHS
KTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHRD
VKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDL
QDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLNV
YLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLLR
YDHQERLTALEAMTHPYFQQVRAAE
3D structure
PDB1m2p Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight
ChainA
Resolution2.0 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 HNA A V45 G46 R47 V53 K68 V95 F113 I174 D175 V39 G40 R41 V47 K62 V89 F107 I168 D169 PDBbind-CN: -logKd/Ki=6.11,Ki=0.78uM
BindingDB: Ki=780nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:1m2p, PDBe:1m2p, PDBj:1m2p
PDBsum1m2p
PubMed12419810
UniProtP28523|CSK2A_MAIZE Casein kinase II subunit alpha (Gene Name=ACK2)

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