Structure of PDB 5cu3 Chain A

Receptor sequence
>5cu3A (length=325) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSE
VFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVK
DPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGI
MHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPEL
LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTE
DLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLD
KLLRYDHQSRLTAREAMEHPYFYTV
3D structure
PDB5cu3 Specific inhibition of CK2 alpha from an anchor outside the active site.
ChainA
Resolution1.787 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 P184 S194
Catalytic site (residue number reindexed from 1) D154 K156 N159 D173 P182 S192
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 54S A K68 F113 N118 F121 L124 L128 Y136 P159 H160 V162 I164 I174 D175 M225 K66 F111 N116 F119 L122 L126 Y134 P157 H158 V160 I162 I172 D173 M223 MOAD: Kd=0.32uM
BindingDB: Kd=320nM,IC50=670nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5cu3, PDBe:5cu3, PDBj:5cu3
PDBsum5cu3
PubMed28451126
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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