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Atomistry » Magnesium » PDB 6wid-6wpj » 6wo1 » |
Magnesium in PDB 6wo1: Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory SubunitEnzymatic activity of Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit
All present enzymatic activity of Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit:
2.2.1.6; Protein crystallography data
The structure of Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit, PDB code: 6wo1
was solved by
L.W.Guddat,
T.Lonhienne,
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 Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit
(pdb code 6wo1). 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 Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit, PDB code: 6wo1: Magnesium binding site 1 out of 1 in 6wo1Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Hybrid Acetohydroxyacid Synthase Complex Structure with Cryptococcus Neoformans Ahas Catalytic Subunit and Saccharomyces Cerevisiae Ahas Regulatory Subunit
![]() Mono view ![]() Stereo pair view
Reference:
T.Lonhienne,
Y.S.Low,
M.D.Garcia,
T.Croll,
Y.Gao,
Q.Wang,
L.Brillault,
C.M.Williams,
J.A.Fraser,
R.P.Mcgeary,
N.P.West,
M.J.Landsberg,
Z.Rao,
G.Schenk,
L.W.Guddat.
Structures of Fungal and Plant Acetohydroxyacid Synthases. Nature V. 586 317 2020.
Page generated: Tue Oct 1 23:03:14 2024
ISSN: ESSN 1476-4687 PubMed: 32640464 DOI: 10.1038/S41586-020-2514-3 |
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