Structure of PDB 6yph Chain B

Receptor sequence
>6yphB (length=327) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMG
IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE
LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT
EDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFL
DKLLRYDHQSRLTAREAMEHPYFYTVV
3D structure
PDB6yph Proposed Allosteric Inhibitors Bind to the ATP Site of CK2 alpha.
ChainB
Resolution1.67 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) D155 K157 N160 D174 S193
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 N5Q B L45 G46 R47 V53 V66 K68 F113 H160 M163 I174 D175 L44 G45 R46 V52 V65 K67 F112 H159 M162 I173 D174 BindingDB: IC50=600nM,Kd=110nM,Ki=180nM
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:6yph, PDBe:6yph, PDBj:6yph
PDBsum6yph
PubMed33119282
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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