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PDBsum entry 3kf7

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protein ligands links
Transferase PDB id
3kf7
Jmol
Contents
Protein chain
337 a.a. *
Ligands
L9G
Waters ×146
* Residue conservation analysis
PDB id:
3kf7
Name: Transferase
Title: Crystal structure of human p38alpha complexed with a triazolopyrimidine compound
Structure: Mitogen-activated protein kinase 14. Chain: a. Synonym: mitogen-activated protein kinase p38 alpha, map ki alpha, cytokine suppressive anti-inflammatory drug-binding csaid-binding protein, csbp, max-interacting protein 2, map mxi2, sapk2a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: csbp, csbp1, csbp2, cspb1, mapk14, mxi2, thp-1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.235     R-free:   0.274
Authors: H.-S.Shieh,J.M.Williams,R.A.Stegeman,L.Xing,K.D.Jerome
Key ref: K.D.Jerome et al. (2010). Continued exploration of the triazolopyridine scaffold as a platform for p38 MAP kinase inhibition. Bioorg Med Chem Lett, 20, 469-473. PubMed id: 19969459 DOI: 10.1016/j.bmcl.2009.11.114
Date:
27-Oct-09     Release date:   29-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q16539  (MK14_HUMAN) -  Mitogen-activated protein kinase 14
Seq:
Struc:
360 a.a.
337 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.24  - Mitogen-activated protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell   8 terms 
  Biological process     intracellular signal transduction   71 terms 
  Biochemical function     nucleotide binding     11 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2009.11.114 Bioorg Med Chem Lett 20:469-473 (2010)
PubMed id: 19969459  
 
 
Continued exploration of the triazolopyridine scaffold as a platform for p38 MAP kinase inhibition.
K.D.Jerome, P.V.Rucker, L.Xing, H.S.Shieh, J.E.Baldus, S.R.Selness, M.A.Letavic, J.F.Braganza, K.F.McClure.
 
  ABSTRACT  
 
The structure based drug design, synthesis and structure-activity relationship of a series of C6 sulfur linked triazolopyridine based p38 inhibitors are described. The metabolic deficiencies of this series were overcome through changes in the C6 linker from sulfur to methylene, which was predicted by molecular modeling to be bioisosteric. X-ray of the ethylene linked compound 61 confirmed the predicted binding orientation of the scaffold in the p38 enzyme.