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PDBsum entry 5i9w

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protein ligands links
Transferase PDB id
5i9w

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
267 a.a.
Ligands
ANP
EDO ×2
Waters ×301
PDB id:
5i9w
Name: Transferase
Title: Crystal structure of ephrin a2 (epha2) receptor protein kinase with anp
Structure: Ephrin type-a receptor 2. Chain: a. Synonym: epithelial cell kinase,tyrosine-protein kinase receptor eck. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: epha2, eck. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9
Resolution:
1.36Å     R-factor:   0.170     R-free:   0.180
Authors: D.Kudlinzki,V.L.Linhard,S.L.Gande,S.Sreeramulu,K.Saxena,S.Heinzlmeir, G.Medard,B.Kuester,H.Schwalbe
Key ref: S.Heinzlmeir et al. (2016). Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs. Acs Chem Biol, 11, 3400-3411. PubMed id: 27768280 DOI: 10.1021/acschembio.6b00709
Date:
21-Feb-16     Release date:   09-Nov-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29317  (EPHA2_HUMAN) -  Ephrin type-A receptor 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
976 a.a.
267 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
+ ATP
= O-phospho-L-tyrosyl-[protein]
Bound ligand (Het Group name = ANP)
matches with 81.25% similarity
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1021/acschembio.6b00709 Acs Chem Biol 11:3400-3411 (2016)
PubMed id: 27768280  
 
 
Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs.
S.Heinzlmeir, D.Kudlinzki, S.Sreeramulu, S.Klaeger, S.L.Gande, V.Linhard, M.Wilhelm, H.Qiao, D.Helm, B.Ruprecht, K.Saxena, G.Médard, H.Schwalbe, B.Kuster.
 
  ABSTRACT  
 
No abstract given.

 

 

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