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Atomistry » Magnesium » PDB 4xgr-4xtj » 4xlv | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 4xgr-4xtj » 4xlv » |
Magnesium in PDB 4xlv: Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase DimerEnzymatic activity of Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer
All present enzymatic activity of Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer:
2.7.10.1; Protein crystallography data
The structure of Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer, PDB code: 4xlv
was solved by
S.R.Hubbard,
S.Li,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer
(pdb code 4xlv). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer, PDB code: 4xlv: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 4xlvGo back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 4xlvGo back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Crystal Structure of the Activated Insulin Receptor Tyrosine Kinase Dimer
![]() Mono view ![]() Stereo pair view
Reference:
M.Z.Cabail,
S.Li,
E.Lemmon,
M.E.Bowen,
S.R.Hubbard,
W.T.Miller.
The Insulin and IGF1 Receptor Kinase Domains Are Functional Dimers in the Activated State. Nat Commun V. 6 6406 2015.
Page generated: Tue Aug 12 03:09:36 2025
ISSN: ESSN 2041-1723 PubMed: 25758790 DOI: 10.1038/NCOMMS7406 |
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