Structure of PDB 5csh Chain B

Receptor sequence
>5cshB (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFQTLTDYDIRFYMYEILKALDYCHSMGIMHR
DVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVD
YQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLY
DYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLL
RYDHQSRLTAREAMEHPYFYTVV
3D structure
PDB5csh Specific inhibition of CK2 alpha from an anchor outside the active site.
ChainB
Resolution1.59 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) D151 K153 N156 D170 P179 S189
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 54E B Y136 P159 V162 I164 Y131 P154 V157 I159 MOAD: Kd=270uM
BindingDB: IC50=500000nM
BS02 54E B W24 H183 Q186 W23 H178 Q181 MOAD: Kd=270uM
BindingDB: IC50=500000nM
BS03 ATP B V53 V66 V116 K158 H160 M163 I174 V52 V65 V115 K153 H155 M158 I169
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:5csh, PDBe:5csh, PDBj:5csh
PDBsum5csh
PubMed28451126
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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