Structure of PDB 5cu2 Chain B

Receptor sequence
>5cu2B (length=325) Species: 9606 (Homo sapiens) [Search protein sequence]
GPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSE
VFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVK
DPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGI
MHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPEL
LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTE
DLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLD
KLLRYDHQSRLTAREAMEHPYFYTV
3D structure
PDB5cu2 A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066.
ChainB
Resolution1.705 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) D154 K156 N159 D173 P182 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 551 B F121 P159 H160 V162 I164 M221 M225 F119 P157 H158 V160 I162 M219 M223
BS02 551 B Y39 L41 I69 V101 D103 T108 A110 Y37 L39 I67 V99 D101 T106 A108
BS03 54G B K68 F113 M163 I174 D175 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:5cu2, PDBe:5cu2, PDBj:5cu2
PDBsum5cu2
PubMed28495381
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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