Structure of PDB 5ctp Chain A

Receptor sequence
>5ctpA (length=324) Species: 9606 (Homo sapiens) [Search protein sequence]
PVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEV
FEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKD
PVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIM
HRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELL
VDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTED
LYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDK
LLRYDHQSRLTAREAMEHPYFYTV
3D structure
PDB5ctp A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066.
ChainA
Resolution2.033 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) 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 54R A P159 H160 V162 M163 I164 M221 M225 P156 H157 V159 M160 I161 M218 M222
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
External links
PDB RCSB:5ctp, PDBe:5ctp, PDBj:5ctp
PDBsum5ctp
PubMed28495381
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

[Back to BioLiP]