Potassium in PDB 5ims: 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: 5ims 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)	42.18 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	95.683, 110.180, 180.005, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 19.3

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 5ims). 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: 5ims:
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:34.7 occ:1.00 O A:HOH1108 2.6 49.4 1.0 O A:TRP508 2.7 31.2 1.0 O A:GLN506 2.7 36.2 1.0 O A:HOH964 2.8 28.3 1.0 O A:HOH822 2.9 44.3 1.0 OE1 A:GLN343 2.9 33.1 1.0 C A:GLN506 3.7 31.6 1.0 CD A:GLN343 3.8 25.9 1.0 C A:TRP508 3.8 30.2 1.0 NE2 A:GLN343 4.0 26.7 1.0 O A:ALA505 4.1 31.0 1.0 OD2 A:ASP350 4.2 49.0 1.0 O A:HOH859 4.2 34.6 1.0 CD1 A:TRP510 4.4 24.5 1.0 CA A:THR509 4.4 33.8 1.0 N A:TRP508 4.4 30.0 1.0 C A:HIS507 4.5 36.0 1.0 N A:HIS507 4.5 29.6 1.0 N A:THR509 4.5 28.7 1.0 CA A:HIS507 4.6 30.4 1.0 CA A:GLN506 4.6 32.6 1.0 NE1 A:TRP510 4.8 28.4 1.0 CG A:ASP350 4.8 42.0 1.0 CA A:TRP508 4.8 24.6 1.0 N A:TRP510 4.9 31.5 1.0 CE2 A:TYR460 4.9 46.8 1.0 O A:HIS507 5.0 36.0 1.0 OG1 A:THR509 5.0 38.5 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:41.7 occ:1.00 O B:TRP508 2.6 31.1 1.0 O B:HOH866 2.7 34.1 1.0 O B:GLN506 2.8 37.9 1.0 NE2 B:GLN343 2.8 31.2 1.0 O B:HOH814 2.8 57.4 1.0 O B:HOH1018 2.9 52.2 1.0 C B:GLN506 3.7 36.3 1.0 CD B:GLN343 3.7 33.4 1.0 C B:TRP508 3.8 34.2 1.0 OE1 B:GLN343 3.9 43.5 1.0 O B:ALA505 4.0 30.3 1.0 O B:HOH828 4.1 48.2 1.0 CD1 B:TRP510 4.2 28.6 1.0 CA B:THR509 4.3 38.4 1.0 OD2 B:ASP350 4.3 69.5 1.0 N B:HIS507 4.4 31.0 1.0 N B:TRP508 4.5 32.3 1.0 N B:THR509 4.5 39.9 1.0 C B:HIS507 4.5 38.8 1.0 CA B:GLN506 4.5 41.1 1.0 CA B:HIS507 4.6 30.4 1.0 NE1 B:TRP510 4.7 27.1 1.0 CG B:ASP350 4.7 58.6 1.0 N B:TRP510 4.8 33.9 1.0 CA B:TRP508 4.8 28.6 1.0 CE2 B:TYR460 4.9 67.4 1.0 O B:HIS507 5.0 33.7 1.0

L.W.Guddat, T.Lonhienne. A Hidden Redox Cycle Controls Catalysis in Acetohydroxyacid Synthase To Be Published.