Structure of PDB 6ehk Chain A

Receptor sequence
>6ehkA (length=327) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSE
VFEAINITNNEKVVVKILKPVAAAKIKREIKILENLRGGPNIITLADIVK
DPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGI
MHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPEL
LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTE
DLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLD
KLLRYDHQSRLTAREAMEHPYFYTVVK
3D structure
PDB6ehk Second-generation CK2 alpha inhibitors targeting the alpha D pocket.
ChainA
Resolution1.4 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) D154 K156 N159 D173 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 AUW A L124 Y125 P159 H160 V162 M163 I164 M221 M225 L122 Y123 P157 H158 V160 M161 I162 M219 M223 BindingDB: IC50=7000nM
BS02 54G A V53 V66 K68 F113 M163 I174 D175 V51 V64 K66 F111 M161 I172 D173 BindingDB: Kd=58000nM
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:6ehk, PDBe:6ehk, PDBj:6ehk
PDBsum6ehk
PubMed29732088
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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