Structure of PDB 1lp4 Chain A

Receptor sequence
>1lp4A (length=327) Species: 4577 (Zea mays) [Search protein sequence]
SKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEG
INVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQHS
KTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHRD
VKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDL
QDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLNV
YLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLLR
YDHQERLTALEAMTHPYFQQVRAAENS
3D structure
PDB1lp4 Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
ChainA
Resolution1.86 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 MG A N161 D175 N155 D169
BS02 ANP A G48 S51 V53 I66 K68 V116 K158 H160 M163 I174 D175 G42 S45 V47 I60 K62 V110 K152 H154 M157 I168 D169
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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Molecular Function
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Cellular Component
External links
PDB RCSB:1lp4, PDBe:1lp4, PDBj:1lp4
PDBsum1lp4
PubMed15740749
UniProtP28523|CSK2A_MAIZE Casein kinase II subunit alpha (Gene Name=ACK2)

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