Potassium in PDB 6bd3: 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: 6bd3 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)	47.31 / 2.28
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	95.898, 108.766, 180.001, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 20.1

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 6bd3). 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: 6bd3:
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:49.4 occ:1.00 O A:GLN506 2.7 52.6 1.0 O A:TRP508 2.7 43.6 1.0 O A:HOH893 2.8 40.1 1.0 OE1 A:GLN343 2.9 47.2 1.0 O A:HOH809 2.9 51.9 1.0 OD2 A:ASP350 3.7 71.6 1.0 CD A:GLN343 3.7 43.9 1.0 C A:GLN506 3.8 55.6 1.0 NE2 A:GLN343 3.9 36.7 1.0 C A:TRP508 3.9 46.6 1.0 O A:ALA505 4.1 44.9 1.0 O A:HOH933 4.2 51.4 1.0 CD1 A:TRP510 4.4 41.4 1.0 N A:TRP508 4.5 48.4 1.0 CA A:THR509 4.5 44.6 1.0 CG A:ASP350 4.5 64.6 1.0 N A:HIS507 4.6 52.2 1.0 C A:HIS507 4.6 51.0 1.0 N A:THR509 4.6 40.1 1.0 CA A:GLN506 4.6 49.5 1.0 CA A:HIS507 4.7 53.4 1.0 NE1 A:TRP510 4.8 43.2 1.0 CA A:TRP508 4.9 44.8 1.0 CE2 A:TYR460 4.9 91.8 1.0 CB A:ASP350 5.0 55.8 1.0 N A:TRP510 5.0 45.8 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:63.7 occ:1.00 O B:TRP508 2.7 58.6 1.0 O B:HOH825 2.8 51.2 1.0 O B:GLN506 2.8 47.0 1.0 OE1 B:GLN343 2.9 58.3 1.0 OD2 B:ASP350 3.4 95.2 1.0 CD B:GLN343 3.7 75.5 1.0 C B:GLN506 3.8 45.9 1.0 NE2 B:GLN343 3.8 58.7 1.0 C B:TRP508 3.9 55.2 1.0 O B:ALA505 4.0 43.7 1.0 CD1 B:TRP510 4.3 41.9 1.0 CG B:ASP350 4.3 92.4 1.0 CA B:THR509 4.5 61.1 1.0 N B:HIS507 4.5 44.1 1.0 CA B:GLN506 4.6 43.1 1.0 N B:TRP508 4.6 44.4 1.0 C B:HIS507 4.6 45.8 1.0 N B:THR509 4.6 57.9 1.0 NE1 B:TRP510 4.7 41.0 1.0 CA B:HIS507 4.7 47.4 1.0 CE2 B:TYR460 4.7 0.6 1.0 CB B:ASP350 4.9 87.4 1.0 N B:TRP510 4.9 51.2 1.0 CA B:TRP508 4.9 49.5 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