Het-PDB Navi2 (PDB: 4FBX)

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Ligands
Code	Name		Style	Show	Link
CL	Chloride ion				PoSSuM

Non-standard Residues
Code	Name	Show

Glycosylation
Code	Name	Emphasize

Modification
Code	Name	Show
0TJ	N-(6-oxohexyl)-2-(4,5,6,7-tetrabromo-1h-benzimidazol-1-yl)acetamide

Download interaction data: 4FBX

Code :

4FBX PDBj RCSB PDB PDBe

Header :

TRANSFERASE/TRANSFERASE INHIBITOR

Title :

Complex structure of human protein kinase CK2 catalytic subunit crystallized in the presence of a bisubstrate inhibitor

Release Data :

2012-10-17

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	bisubstrate inhibitor	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: yes

Authors :

Enkvist, E., Viht, K., Bischoff, N., Vahter, J., Saaver, S., Raidaru, G., Issinger, O.-G., Niefind, K., Uri, A.

Keywords :

protein kinase fold, protein phosphorylation, Bisubstrate inhibitor, TRANSFERASE-TRANSFERASE INHIBITOR complex

Exp. method :

X-RAY DIFFRACTION ( 2.330 Å )

Citation :

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

The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin.

Raaf, J.,Klopffleisch, K.,Issinger, O.G. et al.
(2008) J.Mol.Biol. 377 : 1 - 8

PubMed: 18242640
DOI: 10.1016/j.jmb.2008.01.008

Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights.

Niefind, K.,Raaf, J.,Issinger, O.G.
(2009) Cell.Mol.Life Sci. 66 : 1800 - 1816

PubMed: 19387553
DOI: 10.1007/s00018-009-9149-8

Chain :

UniProt :

P68400 (CSK21_HUMAN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
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

PDB ID: 4FBX

Hetero Atom Contents

Structure summary

Reaction