Brand  (β version)

PDB ID: 6SPX

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Ligands
Code Name Style Show Link
9AB 8-[4,5,6,7-tetrakis(bromanyl)benzimidazol-1-yl]octanoic acid PoSSuM
Non-standard Residues
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DAS D-aspartic acid
Glycosylation
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Structure summary

Code : 6SPX   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Structure of protein kinase CK2 catalytic subunit in complex with the CK2beta-competitive bisubstrate inhibitor ARC1502
Release Data : 2020-01-29
Compound :
mol_id molecule chains synonym
1 Casein kinase II subunit alpha A CK II alpha
ec: 2.7.11.1
mol_id molecule chains
2 ARC1502 B
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: CSNK2A1, CK2A1
mol_id organism_scientific
2 Synthetic construct  (taxid:32630)
synthetic: yes
Authors : Niefind, K., Schnitzler, A.
Keywords : protein kinase CK2 casein kinase 2 bisubstrate inhibitor, transferase
Exp. method : X-RAY DIFFRACTION ( 1.994 Å )
Citation :

Unexpected CK2 beta-antagonistic functionality of bisubstrate inhibitors targeting protein kinase CK2.

Pietsch, M.,Viht, K.,Schnitzler, A.  et al.
(2020)  Bioorg.Chem.  96 : 103608 - 103608

PubMed: 32058103
DOI: 10.1016/j.bioorg.2020.103608

A subnanomolar fluorescent probe for protein kinase CK2 interaction studies.

Enkvist, E.,Viht, K.,Bischoff, N.  et al.
(2012)  Org. Biomol. Chem.  10 : 8645 - 8653

PubMed: 23032938
DOI: 10.1039/c2ob26022k

Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.

Ermakova, I.,Boldyreff, B.,Issinger, O.G.  et al.
(2003)  J. Mol. Biol.  330 : 925 - 934

PubMed: 12860116

Reaction

Chain : A
UniProt : P68400 (CSK21_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 PubMed:20545769, PubMed:20625391, PubMed:21482717, PubMed:22184066, PubMed:23123191, PubMed:30699359, PubMed:30898438, PubMed:31439799
left-to-right PubMed:20545769, PubMed:21482717, PubMed:23123191, PubMed:30699359, PubMed:30898438, PubMed:31439799, PubMed:35597237
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:20625391, PubMed:22325354, PubMed:31439799
left-to-right PubMed:31439799