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PDBsum entry 3r63

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Transferase PDB id
3r63

 

 

 

 

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JSmol PyMol  
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-regulated kinase 2, erk-2, map kinase isoform p42, p42-mapk, mitogen-activated 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
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 from Rattus norvegicus
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:
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    
 
 
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.

 

 

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