Brand  (β version)

PDB ID: 3R0T

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
EDO 1,2-ethanediol PoSSuM
FU9 3-(cyclopropylamino)-5-{[3-(trifluoromethyl)phenyl]amino}pyrimido[4,5-C]quinoline-8-carboxylic acid PoSSuM
PEG Di(hydroxyethyl)ether PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3R0T   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279
Release Data : 2011-12-07
Compound :
mol_id molecule chains synonym
1 Casein kinase II subunit alpha A CK II alpha
ec: 2.7.11.1
fragment: unp residues 1-337
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: CSNK2A1, CK2A1
expression_system_vector_type: plasmid
expression_system_plasmid: pT7-7
Authors : Battistutta, R., Papinutto, E., Lolli, G., Pierre, F., Haddach, M., Ryckman, D.M.
Keywords : Kinase, CK2-inhibitor complex, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.7500 Å )
Citation :

Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical trials for the treatment of cancer.

Battistutta, R.,Cozza, G.,Pierre, F.  et al.
(2011)  Biochemistry  50 : 8478 - 8488

PubMed: 21870818
DOI: 10.1021/bi2008382

Quinalizarin as a potent, selective and cell-permeable inhibitor of protein kinase CK2.

Cozza, G.,Mazzorana, M.,Papinutto, E.  et al.
(2009)  Biochem.J.  421 : 387 - 395

PubMed: 19432557
DOI: 10.1042/BJ20090069

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