Potassium in PDB 6bd9: Saccharomyces Cerevisiae Acetohydroxyacid Synthase

All present enzymatic activity of Saccharomyces Cerevisiae Acetohydroxyacid Synthase:
2.2.1.6;

The structure of Saccharomyces Cerevisiae Acetohydroxyacid Synthase, PDB code: 6bd9 was solved by L.W.Guddat, T.Lonhienne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	96.024, 110.967, 180.244, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 18.1

The structure of Saccharomyces Cerevisiae Acetohydroxyacid Synthase also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Potassium atom in the Saccharomyces Cerevisiae Acetohydroxyacid Synthase (pdb code 6bd9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Saccharomyces Cerevisiae Acetohydroxyacid Synthase, PDB code: 6bd9:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Saccharomyces Cerevisiae Acetohydroxyacid Synthase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Saccharomyces Cerevisiae Acetohydroxyacid Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:K701 b:31.3 occ:1.00 O A:TRP508 2.6 32.2 1.0 O A:HOH1078 2.7 50.4 1.0 O A:GLN506 2.7 31.7 1.0 O A:HOH970 2.8 29.9 1.0 OE1 A:GLN343 2.8 32.0 1.0 O A:HOH836 2.9 47.7 1.0 C A:GLN506 3.7 31.7 1.0 CD A:GLN343 3.7 27.2 1.0 C A:TRP508 3.8 30.1 1.0 NE2 A:GLN343 3.9 25.6 1.0 O A:HOH829 4.1 29.1 1.0 O A:ALA505 4.2 32.5 1.0 OD2 A:ASP350 4.2 49.3 1.0 CA A:THR509 4.3 32.9 1.0 CD1 A:TRP510 4.4 25.6 1.0 C A:HIS507 4.5 30.5 1.0 N A:THR509 4.5 31.0 1.0 N A:TRP508 4.5 26.6 1.0 N A:HIS507 4.5 30.5 1.0 CA A:HIS507 4.6 32.4 1.0 CA A:GLN506 4.6 30.1 1.0 CG A:ASP350 4.8 45.5 1.0 CE2 A:TYR460 4.8 51.0 1.0 NE1 A:TRP510 4.8 26.1 1.0 CA A:TRP508 4.8 28.9 1.0 N A:TRP510 4.8 29.6 1.0 OG1 A:THR509 4.9 37.3 1.0 O A:HIS507 4.9 34.6 1.0

Potassium binding site 2 out of 2 in the Saccharomyces Cerevisiae Acetohydroxyacid Synthase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Saccharomyces Cerevisiae Acetohydroxyacid Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:K701 b:39.2 occ:1.00 O B:TRP508 2.6 34.7 1.0 OE1 B:GLN343 2.8 49.7 1.0 O B:HOH801 2.8 54.7 1.0 O B:GLN506 2.8 37.5 1.0 O B:HOH884 2.8 39.4 1.0 O B:HOH937 2.9 47.1 1.0 CD B:GLN343 3.7 55.9 1.0 C B:GLN506 3.7 35.7 1.0 C B:TRP508 3.7 38.0 1.0 NE2 B:GLN343 4.0 50.3 1.0 O B:ALA505 4.1 34.0 1.0 O B:HOH863 4.1 48.4 1.0 CA B:THR509 4.2 37.1 1.0 CD1 B:TRP510 4.3 30.9 1.0 OD2 B:ASP350 4.3 71.7 1.0 N B:THR509 4.4 38.6 1.0 N B:HIS507 4.5 33.5 1.0 N B:TRP508 4.5 31.6 1.0 C B:HIS507 4.5 35.7 1.0 CA B:GLN506 4.5 35.2 1.0 CA B:HIS507 4.6 36.7 1.0 NE1 B:TRP510 4.7 29.8 1.0 CG B:ASP350 4.7 67.7 1.0 N B:TRP510 4.8 37.4 1.0 CE2 B:TYR460 4.8 75.1 1.0 CA B:TRP508 4.8 31.2 1.0 OG1 B:THR509 4.9 40.6 1.0 O B:HIS507 5.0 36.1 1.0

T.Lonhienne, M.D.Garcia, C.Noble, J.Harmer, J.A.Fraser, C.M.Williams, L.W.Guddat. High Resolution Crystal Structures of the Acetohydroxyacid Synthase-Pyruvate Complex Provide New Insights Into Its Catalytic Mechanism Chemistryselect 2017.
ISSN: ESSN 2365-6549
DOI: 10.1002/SLCT.201702128