Brand  (β version)

PDB ID: 1CKJ

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
WO4 Tungstate(VI)ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1CKJ   PDBj   RCSB PDB   PDBe
Header : PHOSPHOTRANSFERASE
Title : CASEIN KINASE I DELTA TRUNCATION MUTANT CONTAINING RESIDUES 1-317 COMPLEX WITH BOUND TUNGSTATE
Release Data : 1995-12-07
Compound :
mol_id molecule chains
1 RECOMBINANT CASEIN KINASE I DELTA A,B
ec: 2.7.1.-
mutation: C-TERMINAL TRUNCATION MUTANT CONTAINING RESIDUES 1 - 317
Source :
mol_id organism_scientific organism_common expression_system
1 Rattus norvegicus  (taxid:10116) Norway rat Escherichia coli  (taxid:562)
cell_line: 293
organ: TESTES
gene: T7
expression_system_strain: 293
expression_system_vector_type: T7
expression_system_plasmid: PET-8C
expression_system_gene: T7
other_details: HOST BL21(DE3)
Authors : Longenecker, K.L., Roach, P.J., Hurley, T.D.
Keywords : PROTEIN KINASE, PHOSPHOTRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.46 Å )
Citation :

Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition.

Longenecker, K.L.,Roach, P.J.,Hurley, T.D.
(1996)  J.Mol.Biol.  257 : 618 - 631

PubMed: 8648628
DOI: 10.1006/jmbi.1996.0189

Crystal Structure of Casein Kinase-1, a Phosphate-Directed Protein Kinase

Xu, R.,Carmel, G.,Sweet, R.M.  et al.
(1995)  Embo J.  14 : 1015

Molecular Cloning, Expression, and Characterization of a 49-Kilodalton Casein Kinase I Isoform from Rat Testis

Graves, P.R.,Haas, D.W.,Hagedorn, C.H.  et al.
(1993)  J.Biol.Chem.  268 : 6394

Reaction

Chain : A, B
UniProt : Q06486 (KC1D_RAT)
Reaction: EC: Evidence:
Physiological Direction:
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) 2.7.11.1 PubMed:15961172
left-to-right
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) 2.7.11.1 PubMed:15961172
left-to-right
L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H(+) 2.7.11.26 UniProtKB:P48730
left-to-right
L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau protein] + ADP + H(+) 2.7.11.26 UniProtKB:P48730
left-to-right