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PDBsum entry 4b99

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protein ligands links
Transferase PDB id
4b99
Jmol
Contents
Protein chain
335 a.a.
Ligands
R4L
Waters ×9
PDB id:
4b99
Name: Transferase
Title: Crystal structure of mapk7 (erk5) with inhibitor
Structure: Mitogen-activated protein kinase 7. Chain: a. Fragment: kinase domain. Synonym: map kinase 7, mapk 7, big map kinase 1, bmk-1, extracellular signal-regulated kinase 5, erk-5. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Resolution:
2.80Å     R-factor:   0.225     R-free:   0.286
Authors: J.M.Elkins,J.Wang,M.Vollmar,P.Mahajan,P.Savitsky,X.Deng,N.S. A.C.W.Pike,F.Von Delft,C.Bountra,C.Arrowsmith,A.Edwards,S.K
Key ref: J.M.Elkins et al. (2013). X-ray crystal structure of ERK5 (MAPK7) in complex with a specific inhibitor. J Med Chem, 56, 4413-4421. PubMed id: 23656407 DOI: 10.1021/jm4000837
Date:
03-Sep-12     Release date:   19-Sep-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13164  (MK07_HUMAN) -  Mitogen-activated protein kinase 7
Seq:
Struc:
 
Seq:
Struc:
816 a.a.
335 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 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!
  Biological process     protein phosphorylation   1 term 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     5 terms  

 

 
    reference    
 
 
DOI no: 10.1021/jm4000837 J Med Chem 56:4413-4421 (2013)
PubMed id: 23656407  
 
 
X-ray crystal structure of ERK5 (MAPK7) in complex with a specific inhibitor.
J.M.Elkins, J.Wang, X.Deng, M.J.Pattison, J.S.Arthur, T.Erazo, N.Gomez, J.M.Lizcano, N.S.Gray, S.Knapp.
 
  ABSTRACT  
 
No abstract given.