Potassium in PDB 1me9: Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound

All present enzymatic activity of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound:
1.1.1.205;

The structure of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound, PDB code: 1me9 was solved by G.L.Prosise, H.Luecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.77 / 2.20
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	154.412, 154.412, 154.412, 90.00, 90.00, 90.00
R / Rfree (%)	24.8 / 27.3

The binding sites of Potassium atom in the Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound (pdb code 1me9). 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 Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound, PDB code: 1me9:

Potassium binding site 1 out of 1 in the Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:K900 b:35.5 occ:0.75 OD2 A:ASP264 2.5 29.1 1.0 O A:PHE266 2.7 29.1 1.0 O A:HOH902 2.9 0.5 1.0 OD1 A:ASP264 2.9 27.0 1.0 CG A:ASP264 3.1 29.8 1.0 C A:PHE266 3.7 29.9 1.0 CB A:PHE266 3.7 27.0 1.0 CA A:PHE266 4.2 28.1 1.0 CG A:PHE266 4.5 28.1 1.0 N A:PHE266 4.6 27.2 1.0 CB A:ASP264 4.6 29.6 1.0 N A:SER267 4.7 31.5 1.0 O A:HOH908 4.9 28.9 1.0 CD2 A:PHE266 5.0 25.8 1.0

G.L.Prosise, H.Luecke. Crystal Structures of Tritrichomonas Foetus Inosine Monophosphate Dehydrogenase in Complex with Substrate, Cofactor and Analogs: A Structural Basis For the Random-in Ordered-Out Kinetic Mechanism J.Mol.Biol. V. 326 517 2003.
ISSN: ISSN 0022-2836
PubMed: 12559919
DOI: 10.1016/S0022-2836(02)01383-9