Structure of PDB 3at4 Chain A

Receptor sequence
>3at4A (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
SGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYS
EVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIV
KDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMG
IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPE
LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT
EDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFL
DKLLRYDHQSRLTAREAMEHPYFYTVVKDQA
3D structure
PDB3at4 A detailed thermodynamic profile of cyclopentyl and isopropyl derivatives binding to CK2 kinase
ChainA
Resolution2.2 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) 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 CCK A L45 V53 V66 K68 F113 H115 V116 M163 I174 D175 L44 V52 V65 K67 F112 H114 V115 M162 I173 D174 MOAD: Kd=2.26nM
PDBbind-CN: -logKd/Ki=8.10,IC50=8.0nM
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:3at4, PDBe:3at4, PDBj:3at4
PDBsum3at4
PubMed21735094
UniProtP68400|CSK21_HUMAN Casein kinase II subunit alpha (Gene Name=CSNK2A1)

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