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PDBsum entry 3zu7

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protein Protein-protein interface(s) links
Transferase/de novo protein PDB id
3zu7
Jmol
Contents
Protein chains
344 a.a.
154 a.a.
Waters ×236
PDB id:
3zu7
Name: Transferase/de novo protein
Title: Crystal structure of a designed selected ankyrin repeat protein in complex with the map kinase erk2
Structure: Mitogen-activated protein kinase 1. Chain: a. Fragment: residues 3-358. Synonym: map kinase 1, mapk 1, ert1, extracellular signal-r kinase 2, erk-2, map kinase isoform p42, p42-mapk, mitogen-activated protein kinase 2, map kinase 2, mapk 2. Engineered: yes. Designed ankyrin repeat protein. Chain: b.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic construct. Organism_taxid: 32630. Expression_system_taxid: 83333. Expression_system_variant: xl1-blue.
Resolution:
1.97Å     R-factor:   0.221     R-free:   0.269
Authors: L.Kummer,P.R.Mittl,A.Pluckthun
Key ref: L.Kummer et al. (2012). Structural and functional analysis of phosphorylation-specific binders of the kinase ERK from designed ankyrin repeat protein libraries. Proc Natl Acad Sci U S A, 109, E2248. PubMed id: 22843676 DOI: 10.1073/pnas.1205399109
Date:
16-Jul-11     Release date:   27-Jun-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P63086  (MK01_RAT) -  Mitogen-activated protein kinase 1
Seq:
Struc:
358 a.a.
344 a.a.
Protein chain
No UniProt id for this chain
Struc: 154 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: 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: 10.1073/pnas.1205399109 Proc Natl Acad Sci U S A 109:E2248 (2012)
PubMed id: 22843676  
 
 
Structural and functional analysis of phosphorylation-specific binders of the kinase ERK from designed ankyrin repeat protein libraries.
L.Kummer, P.Parizek, P.Rube, B.Millgramm, A.Prinz, P.R.Mittl, M.Kaufholz, B.Zimmermann, F.W.Herberg, A.Plückthun.
 
  ABSTRACT  
 
No abstract given.