Potassium in PDB 6deq: Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam

Enzymatic activity of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam

All present enzymatic activity of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam:
2.2.1.6;

Protein crystallography data

The structure of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam, PDB code: 6deq 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)*	44.21 / 2.13
*Space group*	P 6₂ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	176.536, 176.536, 177.785, 90.00, 90.00, 120.00
*R / R_free (%)*	14.2 / 16.1

Other elements in 6deq:

The structure of Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam also contains other interesting chemical elements:

Fluorine	(F)	10 atoms
Magnesium	(Mg)	1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam (pdb code 6deq). 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 in Complex with the Herbicide Penoxsulam, PDB code: 6deq:

Potassium binding site 1 out of 1 in 6deq

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Potassium Binding Sites List in 6deq

Potassium binding site 1 out of 1 in the Crystal Structure of Candida Albicans Acetohydroxyacid Synthase in Complex with the Herbicide Penoxsulam

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 in Complex with the Herbicide Penoxsulam within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K702 b:32.4 occ:1.00	O	A:PHE504	2.7	25.6	1.0
	O	A:HOH842	2.8	29.7	1.0
	O	A:GLN502	2.8	27.7	1.0
	OD1	A:ASP346	2.8	31.9	1.0
	OE1	A:GLN339	2.8	26.8	1.0
	O	A:HOH1316	2.8	46.1	1.0
	O	A:HOH1243	3.4	47.5	1.0
	CD	A:GLN339	3.6	26.3	1.0
	CG	A:ASP346	3.7	32.1	1.0
	OD2	A:ASP346	3.8	27.8	1.0
	C	A:GLN502	3.8	34.4	1.0
	NE2	A:GLN339	3.8	25.3	1.0
	C	A:PHE504	3.9	29.5	1.0
	O	A:HOH1204	3.9	76.3	1.0
	O	A:ALA501	4.1	24.1	1.0
	CD1	A:TRP506	4.2	22.4	1.0
	CA	A:THR505	4.4	28.8	1.0
	N	A:HIS503	4.6	23.5	1.0
	N	A:THR505	4.6	24.4	1.0
	CA	A:GLN502	4.6	27.9	1.0
	NE1	A:TRP506	4.7	26.1	1.0
	N	A:PHE504	4.7	23.9	1.0
	CE2	A:TYR456	4.7	25.9	1.0
	C	A:HIS503	4.7	28.5	1.0
	CA	A:HIS503	4.8	28.2	1.0
	O	A:HOH1254	4.9	61.5	1.0
	N	A:TRP506	4.9	28.3	1.0
	CA	A:PHE504	4.9	26.4	1.0
	CG	A:GLN339	5.0	22.8	1.0
	O	A:HOH966	5.0	38.7	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 15:45:50 2024

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