Structure of PDB 6ypn Chain B

Receptor sequence
>6ypnB (length=326) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMG
IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE
LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT
EDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFL
DKLLRYDHQSRLTAREAMEHPYFYTV
3D structure
PDB6ypn Proposed Allosteric Inhibitors Bind to the ATP Site of CK2 alpha.
ChainB
Resolution1.58 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 ADP B S51 V53 V66 K68 V116 H160 M163 I174 D175 S50 V52 V65 K67 V115 H159 M162 I173 D174
BS02 ADP B Y50 K77 R80 R155 L178 N189 R191 Y49 K76 R79 R154 L177 N188 R190
BS03 MG B N161 D175 N160 D174
BS04 PO4 B D156 K158 N161 D175 D155 K157 N160 D174
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
View graph for
Biological Process
External links
PDB RCSB:6ypn, PDBe:6ypn, PDBj:6ypn
PDBsum6ypn
PubMed33119282
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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