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PDBsum entry 2ewa

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Transferase PDB id
2ewa

 

 

 

 

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Contents
Protein chain
330 a.a. *
Ligands
SB2
Waters ×73
* Residue conservation analysis
PDB id:
2ewa
Name: Transferase
Title: Dual binding mode of pyridinylimidazole to map kinase p38
Structure: Mitogen-activated protein kinase 14. Chain: a. Synonym: mitogen-activated protein kinase p38 alpha, map kinase p38 alpha, crk1. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: mapk14, crk1, csbp1, csbp2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.10Å     R-factor:   0.241     R-free:   0.279
Authors: L.Delarbre,S.Pouzieux,J.-P.Guilloteau,N.Michot
Key ref: M.Vogtherr et al. (2006). NMR characterization of kinase p38 dynamics in free and ligand-bound forms. Angew Chem Int Ed Engl, 45, 993-997. PubMed id: 16374788
Date:
02-Nov-05     Release date:   01-Aug-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P47811  (MK14_MOUSE) -  Mitogen-activated protein kinase 14 from Mus musculus
Seq:
Struc:
360 a.a.
330 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.24  - mitogen-activated protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Angew Chem Int Ed Engl 45:993-997 (2006)
PubMed id: 16374788  
 
 
NMR characterization of kinase p38 dynamics in free and ligand-bound forms.
M.Vogtherr, K.Saxena, S.Hoelder, S.Grimme, M.Betz, U.Schieborr, B.Pescatore, M.Robin, L.Delarbre, T.Langer, K.U.Wendt, H.Schwalbe.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20141838 B.Yu, I.R.Martins, P.Li, G.K.Amarasinghe, J.Umetani, M.E.Fernandez-Zapico, D.D.Billadeau, M.Machius, D.R.Tomchick, and M.K.Rosen (2010).
Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1.
  Cell, 140, 246-256.
PDB code: 3ky9
19965870 J.M.Steichen, G.H.Iyer, S.Li, S.A.Saldanha, M.S.Deal, V.L.Woods, and S.S.Taylor (2010).
Global consequences of activation loop phosphorylation on protein kinase A.
  J Biol Chem, 285, 3825-3832.  
21095574 L.M.Wodicka, P.Ciceri, M.I.Davis, J.P.Hunt, M.Floyd, S.Salerno, X.H.Hua, J.M.Ford, R.C.Armstrong, P.P.Zarrinkar, and D.K.Treiber (2010).
Activation state-dependent binding of small molecule kinase inhibitors: structural insights from biochemistry.
  Chem Biol, 17, 1241-1249.  
20336692 M.Rabiller, M.Getlik, S.Klüter, A.Richters, S.Tückmantel, J.R.Simard, and D.Rauh (2010).
Proteus in the world of proteins: conformational changes in protein kinases.
  Arch Pharm (Weinheim), 343, 193-206.  
21134636 R.Akella, X.Min, Q.Wu, K.H.Gardner, and E.J.Goldsmith (2010).
The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solution.
  Structure, 18, 1571-1578.
PDB code: 3p4k
20160879 R.S.Armen, J.Chen, and C.L.Brooks (2009).
An Evaluation of Explicit Receptor Flexibility in Molecular Docking Using Molecular Dynamics and Torsion Angle Molecular Dynamics.
  J Chem Theory Comput, 5, 2909-2923.  
19306398 Y.Li, and A.G.Palmer (2009).
Domain swapping in the kinase superfamily: OSR1 joins the mix.
  Protein Sci, 18, 678-681.  
19109437 Y.Shan, M.A.Seeliger, M.P.Eastwood, F.Frank, H.Xu, M.Ã.˜.Jensen, R.O.Dror, J.Kuriyan, and D.E.Shaw (2009).
A conserved protonation-dependent switch controls drug binding in the Abl kinase.
  Proc Natl Acad Sci U S A, 106, 139-144.  
18297096 K.Mihara, C.Almansa, R.L.Smeets, E.E.Loomans, J.Dulos, P.M.Vink, M.Rooseboom, H.Kreutzer, F.Cavalcanti, A.M.Boots, and R.L.Nelissen (2008).
A potent and selective p38 inhibitor protects against bone damage in murine collagen-induced arthritis: a comparison with neutralization of mouse TNFalpha.
  Br J Pharmacol, 154, 153-164.  
17292838 J.Eswaran, W.H.Lee, J.E.Debreczeni, P.Filippakopoulos, A.Turnbull, O.Fedorov, S.W.Deacon, J.R.Peterson, and S.Knapp (2007).
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.
  Structure, 15, 201-213.
PDB codes: 2bva 2c30 2cdz 2f57
17828465 M.Tonelli, L.R.Masterson, K.Hallenga, G.Veglia, and J.L.Markley (2007).
Carbonyl carbon label selective (CCLS) 1H-15N HSQC experiment for improved detection of backbone 13C-15N cross peaks in larger proteins.
  J Biomol NMR, 39, 177-185.  
16640460 N.M.Levinson, O.Kuchment, K.Shen, M.A.Young, M.Koldobskiy, M.Karplus, P.A.Cole, and J.Kuriyan (2006).
A Src-like inactive conformation in the abl tyrosine kinase domain.
  PLoS Biol, 4, e144.
PDB codes: 2g1t 2g2f 2g2h 2g2i
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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