Structure of PDB 5mo8 Chain A

Receptor sequence
>5mo8A (length=325) Species: 9606 (Homo sapiens) [Search protein sequence]
PVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEV
FEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKD
PVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIM
HRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELL
VDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTED
LYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDK
LLRYDHQSRLTAREAMEHPYFYTVV
3D structure
PDB5mo8 A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066.
ChainA
Resolution1.82 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) D153 K155 N158 D172 P181 S191
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 C98 A V66 K68 F113 N118 F121 P159 H160 V162 M163 I164 I174 D175 M225 V63 K65 F110 N115 F118 P156 H157 V159 M160 I161 I171 D172 M222 MOAD: Kd=1.64uM
PDBbind-CN: -logKd/Ki=5.79,Kd=1.64uM
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:5mo8, PDBe:5mo8, PDBj:5mo8
PDBsum5mo8
PubMed28495381
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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