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Atomistry » Magnesium » PDB 5hr6-5i8q » 5hvk | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5hr6-5i8q » 5hvk » |
Magnesium in PDB 5hvk: Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1Enzymatic activity of Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1
All present enzymatic activity of Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1:
2.7.11.1; Protein crystallography data
The structure of Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1, PDB code: 5hvk
was solved by
S.Hamill,
T.J.Boggon,
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 LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1
(pdb code 5hvk). 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 LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1, PDB code: 5hvk: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 5hvkGo back to Magnesium Binding Sites List in 5hvk
Magnesium binding site 1 out
of 2 in the Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 5hvkGo back to Magnesium Binding Sites List in 5hvk
Magnesium binding site 2 out
of 2 in the Crystal Structure of LIMK1 Mutant D460N in Complex with Full-Length Cofilin-1
Mono view Stereo pair view
Reference:
S.Hamill,
H.J.Lou,
B.E.Turk,
T.J.Boggon.
Structural Basis For Noncanonical Substrate Recognition of Cofilin/Adf Proteins By Lim Kinases. Mol.Cell V. 62 397 2016.
Page generated: Mon Dec 14 20:28:58 2020
ISSN: ISSN 1097-2765 PubMed: 27153537 DOI: 10.1016/J.MOLCEL.2016.04.001 |
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