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PDBsum entry 3d7z

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protein ligands links
Transferase PDB id
3d7z
Jmol
Contents
Protein chain
349 a.a. *
Ligands
SO4
GK5
GOL
Waters ×365
* Residue conservation analysis
PDB id:
3d7z
Name: Transferase
Title: Crystal structure of p38 kinase in complex with a biphenyl a inhibitor
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: mapk14, csbp, csbp1, csbp2, cspb1, mxi2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.177     R-free:   0.227
Authors: D.O.Somers,S.Patel
Key ref: R.Angell et al. (2008). Biphenyl amide p38 kinase inhibitors 3: Improvement of cellular and in vivo activity. Bioorg Med Chem Lett, 18, 4428-4432. PubMed id: 18614366 DOI: 10.1016/j.bmcl.2008.06.048
Date:
22-May-08     Release date:   22-Jul-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q16539  (MK14_HUMAN) -  Mitogen-activated protein kinase 14
Seq:
Struc:
360 a.a.
349 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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.2008.06.048 Bioorg Med Chem Lett 18:4428-4432 (2008)
PubMed id: 18614366  
 
 
Biphenyl amide p38 kinase inhibitors 3: Improvement of cellular and in vivo activity.
R.Angell, N.M.Aston, P.Bamborough, J.B.Buckton, S.Cockerill, S.J.deBoeck, C.D.Edwards, D.S.Holmes, K.L.Jones, D.I.Laine, S.Patel, P.A.Smee, K.J.Smith, D.O.Somers, A.L.Walker.
 
  ABSTRACT  
 
The biphenyl amides (BPAs) are a novel series of p38alpha MAP kinase inhibitor. The optimisation of the series to give compounds that are potent in an in vivo disease model is discussed. SAR is presented and rationalised with reference to the crystallographic binding mode.
 

 

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