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PDBsum entry 5ia1

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protein ligands links
Transferase PDB id
5ia1

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
261 a.a.
Ligands
ZZL
EDO
Waters ×136
PDB id:
5ia1
Name: Transferase
Title: Crystal structure of ephrin a2 (epha2) receptor protein kinase with mln8054
Structure: Ephrin type-a receptor 2. Chain: a. Fragment: unp residues 596-900. 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:
2.04Å     R-factor:   0.183     R-free:   0.223
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.
261 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]
+ 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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