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Atomistry » Fluorine » PDB 5hu1-5iev » 5ia1 » |
Fluorine in PDB 5ia1: Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054Enzymatic activity of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054
All present enzymatic activity of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054:
2.7.10.1; Protein crystallography data
The structure of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054, PDB code: 5ia1
was solved by
D.Kudlinzki,
V.L.Linhard,
S.L.Gande,
S.Sreeramulu,
K.Saxena,
S.Heinzlmeir,
G.Medard,
B.Kuester,
H.Schwalbe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ia1:
The structure of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054
(pdb code 5ia1). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054, PDB code: 5ia1: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 5ia1Go back to Fluorine Binding Sites List in 5ia1
Fluorine binding site 1 out
of 2 in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 5ia1Go back to Fluorine Binding Sites List in 5ia1
Fluorine binding site 2 out
of 2 in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054
Mono view Stereo pair view
Reference:
S.Heinzlmeir,
D.Kudlinzki,
S.Sreeramulu,
S.Klaeger,
S.L.Gande,
V.Linhard,
M.Wilhelm,
H.Qiao,
D.Helm,
B.Ruprecht,
K.Saxena,
G.Medard,
H.Schwalbe,
B.Kuster.
Chemical Proteomics and Structural Biology Define EPHA2 Inhibition By Clinical Kinase Drugs. Acs Chem. Biol. V. 11 3400 2016.
Page generated: Sun Dec 13 12:24:28 2020
ISSN: ESSN 1554-8937 PubMed: 27768280 DOI: 10.1021/ACSCHEMBIO.6B00709 |
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