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Magnesium in PDB 6dek: Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit

Enzymatic activity of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit

All present enzymatic activity of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit:
2.2.1.6;

Protein crystallography data

The structure of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit, PDB code: 6dek was solved by M.D.Garcia, L.W.Guddat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.13 / 2.97
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 176.039, 176.039, 177.626, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 18.6

Other elements in 6dek:

The structure of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit also contains other interesting chemical elements:

Potassium (K) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit (pdb code 6dek). 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 Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit, PDB code: 6dek:

Magnesium binding site 1 out of 1 in 6dek

Go back to Magnesium Binding Sites List in 6dek
Magnesium binding site 1 out of 1 in the Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg703

b:44.4
occ:1.00
 O1B A:TPP704 2.0 40.4 1.0
O A:GLU575 2.1 47.8 1.0
OD1 A:ASN573 2.1 55.8 1.0
O2A A:TPP704 2.1 44.0 1.0
OD1 A:ASP546 2.2 42.7 1.0
O A:HOH814 2.2 34.8 1.0
CG A:ASN573 3.0 47.5 1.0
CG A:ASP546 3.2 40.7 1.0
ND2 A:ASN573 3.3 46.6 1.0
C A:GLU575 3.3 48.5 1.0
PB A:TPP704 3.3 47.4 1.0
PA A:TPP704 3.3 43.6 1.0
OD2 A:ASP546 3.5 42.1 1.0
O3A A:TPP704 3.8 54.2 1.0
N A:GLU575 4.0 59.1 1.0
N A:GLY577 4.0 54.6 1.0
O7 A:TPP704 4.0 51.9 1.0
O2B A:TPP704 4.0 43.0 1.0
N A:ASP546 4.0 39.3 1.0
N A:GLN576 4.2 47.0 1.0
CA A:GLU575 4.2 53.7 1.0
O A:LEU571 4.2 53.9 1.0
CA A:GLN576 4.3 47.8 1.0
CB A:ASN573 4.4 42.3 1.0
O3B A:TPP704 4.4 35.0 1.0
CG A:GLU575 4.4 57.5 1.0
N A:ASN573 4.5 47.3 1.0
N A:ALA547 4.5 39.9 1.0
O1A A:TPP704 4.5 35.1 1.0
CB A:ASP546 4.5 38.9 1.0
C A:GLN576 4.7 49.5 1.0
CA A:GLY545 4.7 36.7 1.0
CA A:ASP546 4.8 35.1 1.0
N A:GLU574 4.8 53.5 1.0
CA A:ASN573 4.8 46.9 1.0
C A:GLY545 4.8 43.7 1.0
C A:ASN573 4.9 51.6 1.0
CA A:GLY577 4.9 53.9 1.0
CB A:GLU575 5.0 51.9 1.0
CB A:ALA547 5.0 32.5 1.0

Reference:

M.D.Garcia, S.M.H.Chua, Y.S.Low, Y.T.Lee, K.Agnew-Francis, J.G.Wang, A.Nouwens, T.Lonhienne, C.M.Williams, J.A.Fraser, L.W.Guddat. Commercial Ahas-Inhibiting Herbicides Are Promising Drug Leads For the Treatment of Human Fungal Pathogenic Infections. Proc. Natl. Acad. Sci. V. 115 E9649 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30249642
DOI: 10.1073/PNAS.1809422115
Page generated: Mon Sep 30 23:08:14 2024

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