Brand  (β version)

  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
0OA (1r,2s,3r,4s,6s)-6-(cyclohexylmethoxy)-2,3,4-trihydroxycyclohexyl (2r)-2-methoxy-3-(octadecyloxy)propyl hydrogen (S)-phosphate
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 4E8A   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : The crystal structure of p38a MAP kinase in complex with PIA24
Release Data : 2012-10-31
Compound :
mol_id molecule chains synonym
1 Mitogen-activated protein kinase 14 A MAP kinase 14, MAPK 14, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAP kinase MXI2, MAX-interacting protein 2, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Stress-activated protein kinase 2a, SAPK2a
ec: 2.7.11.24
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A
expression_system_strain: Rosetta
expression_system_vector_type: Plasmid
expression_system_plasmid: pET28
Authors : Livnah, O., Tzarum, N., Eisenberg-Domovich, Y.
Keywords : MAP kinase, p38, signal transduction, alternative activation modes, lipid binding site, PIA, perifosine, Kinase, phosphorylation, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.70 Å )
Citation :

Lipid Molecules Induce p38 alpha Activation via a Novel Molecular Switch.

Tzarum, N.,Eisenberg-Domovich, Y.,Gills, J.J.  et al.
(2012)  J.Mol.Biol.  424 : 339 - 353

PubMed: 23079240
DOI: 10.1016/j.jmb.2012.10.007

Chain : A
UniProt : Q16539 (MK14_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.24 PubMed:11010976, PubMed:35857590
left-to-right
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.24 PubMed:11010976, PubMed:35857590
left-to-right PubMed:11010976, PubMed:35857590