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Atomistry » Magnesium » PDB 1iah-1iru » 1iah | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1iah-1iru » 1iah » |
Magnesium in PDB 1iah: Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex)Enzymatic activity of Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex)
All present enzymatic activity of Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex):
2.7.1.37; Protein crystallography data
The structure of Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex), PDB code: 1iah
was solved by
H.Yamaguchi,
M.Matsushita,
A.C.Nairn,
J.Kuriyan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1iah:
The structure of Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex)
(pdb code 1iah). 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 Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex), PDB code: 1iah: Magnesium binding site 1 out of 1 in 1iahGo back to Magnesium Binding Sites List in 1iah
Magnesium binding site 1 out
of 1 in the Crystal Structure of the Atypical Protein Kinase Domain of A Trp Ca-Channel, Chak (Adp-Mg Complex)
Mono view Stereo pair view
Reference:
H.Yamaguchi,
M.Matsushita,
A.C.Nairn,
J.Kuriyan.
Crystal Structure of the Atypical Protein Kinase Domain of A Trp Channel with Phosphotransferase Activity. Mol.Cell V. 7 1047 2001.
Page generated: Mon Dec 14 06:03:38 2020
ISSN: ISSN 1097-2765 PubMed: 11389851 DOI: 10.1016/S1097-2765(01)00256-8 |
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