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Potassium 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:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium 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 Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Candida Albicans Acetohydroxyacid Synthase Catalytic Subunit, PDB code: 6dek:

Potassium binding site 1 out of 1 in 6dek

Go back to Potassium Binding Sites List in 6dek
Potassium 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 Potassium with other atoms in the K 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:K702

b:60.8
occ:1.00
 O A:PHE504 2.7 59.7 1.0
O A:GLN502 2.8 59.3 1.0
OD1 A:ASP346 2.8 78.6 1.0
O A:HOH817 2.8 54.2 1.0
OE1 A:GLN339 2.9 55.3 1.0
O A:HOH884 2.9 65.0 1.0
CD A:GLN339 3.5 51.8 1.0
NE2 A:GLN339 3.6 47.5 1.0
CG A:ASP346 3.7 78.2 1.0
OD2 A:ASP346 3.8 68.0 1.0
C A:GLN502 3.8 49.5 1.0
C A:PHE504 3.9 54.7 1.0
O A:ALA501 4.1 49.1 1.0
CD1 A:TRP506 4.2 40.7 1.0
CA A:THR505 4.5 43.6 1.0
NE1 A:TRP506 4.6 35.1 1.0
N A:HIS503 4.6 39.9 1.0
CA A:GLN502 4.6 45.8 1.0
CE2 A:TYR456 4.6 57.6 1.0
O A:HOH871 4.6 53.0 1.0
N A:PHE504 4.6 42.7 1.0
C A:HIS503 4.6 54.2 1.0
N A:THR505 4.7 50.6 1.0
CA A:HIS503 4.8 47.2 1.0
CG A:GLN339 4.9 45.1 1.0
CA A:PHE504 4.9 42.8 1.0
N A:TRP506 5.0 43.7 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 Aug 12 15:45:03 2024

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