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PDBsum entry 3r63

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protein links
Transferase PDB id
3r63
Jmol
Contents
Protein chain
347 a.a.
Waters ×161
PDB id:
3r63
Name: Transferase
Title: Structure of erk2 (spe) mutant (s246e)
Structure: Mitogen-activated protein kinase 1. Chain: a. Synonym: map kinase 1, mapk 1, ert1, extracellular signal-r kinase 2, erk-2, map kinase isoform p42, p42-mapk, mitogen- protein kinase 2, map kinase 2, mapk 2. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: mapk1, erk2, mapk, prkm1. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.191     R-free:   0.245
Authors: O.Livnah,Y.Karamansha
Key ref: A.Plotnikov et al. (2011). Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated by autophosphorylation. Mol Cell Biol, 31, 3515-3530. PubMed id: 21730285 DOI: 10.1128/MCB.05424-11
Date:
21-Mar-11     Release date:   17-Aug-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P63086  (MK01_RAT) -  Mitogen-activated protein kinase 1
Seq:
Struc:
358 a.a.
347 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     mitotic spindle   21 terms 
  Biological process     intracellular signal transduction   40 terms 
  Biochemical function     nucleotide binding     15 terms  

 

 
    reference    
 
 
DOI no: 10.1128/MCB.05424-11 Mol Cell Biol 31:3515-3530 (2011)
PubMed id: 21730285  
 
 
Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated by autophosphorylation.
A.Plotnikov, D.Chuderland, Y.Karamansha, O.Livnah, R.Seger.
 
  ABSTRACT  
 
No abstract given.