PDBsum entry 6tgu

Transferase

PDB id: 6tgu

Contents

Protein chain

327 a.a.

Ligands

N92

EDO ×7

Waters ×432

PDB id:

6tgu

Name:

Transferase

Title:

Crystal structure of human protein kinase ck2alpha'(csnk2a2 gene product) in complex with the 2-aminothiazole-type inhibitor cl-oh-3

Structure:

Casein kinase ii subunit alpha'. Chain: a. Synonym: ck ii alpha'. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: csnk2a2, ck2a2. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

0.83Å R-factor: 0.144 R-free: 0.167

Authors:

K.Niefind,D.Lindenblatt,J.Jose,V.M.Applegate,A.Nickelsen

Key ref:

D.Lindenblatt et al. (2020). Structural and Mechanistic Basis of the Inhibitory Potency of Selected 2-Aminothiazole Compounds on Protein Kinase CK2. J Med Chem, 63, 7766-7772. PubMed id: 32589844 DOI: 10.1021/acs.jmedchem.0c00587

Date:

18-Nov-19 Release date: 08-Jul-20

Protein chain

P19784  (CSK22_HUMAN) -  Casein kinase II subunit alpha' from Homo sapiens

Seq: 350 a.a.

Struc: 327 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1021/acs.jmedchem.0c00587

J Med Chem 63:7766-7772 (2020)

PubMed id: 32589844

Structural and Mechanistic Basis of the Inhibitory Potency of Selected 2-Aminothiazole Compounds on Protein Kinase CK2.

D.Lindenblatt, A.Nickelsen, V.M.Applegate, J.Jose, K.Niefind.

ABSTRACT

Selective inhibitors of protein kinase CK2 with significant cytotoxicity on tumor cells based on a 2-aminothiazole scaffold were described recently. Here, these studies are supplemented with representative CK2α/CK2α' complex structures. They reveal that the 2-aminothiazole-based inhibitors occupy the ATP cavity, whereas preliminary data had indicated an allosteric binding site. The crystal structure findings are corroborated by subsequent enzyme kinetic studies; their atomic-resolution quality provides the basis for future optimization of these promising CK2 inhibitors.