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Atomistry » Magnesium » PDB 2f6y-2fl2 » 2fjm | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2f6y-2fl2 » 2fjm » |
Magnesium in PDB 2fjm: The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2Enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2
All present enzymatic activity of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2:
3.1.3.48; Protein crystallography data
The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2, PDB code: 2fjm
was solved by
E.Asante-Appiah,
S.Patel,
C.Desponts,
J.M.Taylor,
C.Lau,
C.Dufresne,
M.Therien,
R.Friesen,
J.W.Becker,
Y.Leblanc,
G.Scapin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2fjm:
The structure of The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2
(pdb code 2fjm). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2, PDB code: 2fjm: Magnesium binding site 1 out of 1 in 2fjmGo back to Magnesium Binding Sites List in 2fjm
Magnesium binding site 1 out
of 1 in the The Structure of Phosphotyrosine Phosphatase 1B in Complex with Compound 2
Mono view Stereo pair view
Reference:
E.Asante-Appiah,
S.Patel,
C.Desponts,
J.M.Taylor,
C.Lau,
C.Dufresne,
M.Therien,
R.Friesen,
J.W.Becker,
Y.Leblanc,
B.P.Kennedy,
G.Scapin.
Conformation-Assisted Inhibition of Protein-Tyrosine Phosphatase-1B Elicits Inhibitor Selectivity Over T-Cell Protein-Tyrosine Phosphatase. J.Biol.Chem. V. 281 8010 2006.
Page generated: Mon Dec 14 07:22:56 2020
ISSN: ISSN 0021-9258 PubMed: 16407290 DOI: 10.1074/JBC.M511827200 |
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