BioLiP

Structure of PDB 5cx9 Chain B

Receptor sequence

>5cx9B (length=325) Species: 9606 (Homo sapiens) [Search protein sequence]

GPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSE
VFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVK
DPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGI
MHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPEL
LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTE
DLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLD
KLLRYDHQSRLTAREAMEHPYFYTV

3D structure

PDB

5cx9 A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066.

Chain

Resolution

1.732 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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	L45 F121 P159 H160 V162 I164 M221 M225	L43 F119 P157 H158 V160 I162 M219 M223
BS02	551	B	Q36 Y39 D103 T108	Q34 Y37 D101 T106

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

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:5cx9, PDBe:5cx9, PDBj:5cx9
PDBsum	5cx9
PubMed	28495381
UniProt	P68400\|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)