Structure of PDB 5cu0 Chain A

Receptor sequence
>5cu0A (length=327) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMG
IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE
LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT
EDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFL
DKLLRYDHQSRLTAREAMEHPYFYTVV
3D structure
PDB5cu0 A fragment-based approach leading to the discovery of a novel binding site and the selective CK2 inhibitor CAM4066.
ChainA
Resolution2.18 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) D155 K157 N160 D174 P183 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 54R A N118 Y136 M137 P159 H160 V162 I164 M221 M225 N117 Y135 M136 P158 H159 V161 I163 M220 M224
BS02 54R A D37 Y39 I69 D103 T108 D36 Y38 I68 D102 T107
BS03 54G A V53 V66 K68 F113 M163 I174 D175 V52 V65 K67 F112 M162 I173 D174 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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5cu0, PDBe:5cu0, PDBj:5cu0
PDBsum5cu0
PubMed28495381
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

[Back to BioLiP]