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

Enzymatic activity of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp and Moa Bound

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

Protein crystallography data

The structure of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp and Moa Bound, PDB code: 1meh 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) 19.98 / 1.95
Space group P 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 153.480, 153.480, 153.480, 90.00, 90.00, 90.00
R / Rfree (%) 24.3 / 27.2

Potassium Binding Sites:

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

Potassium binding site 1 out of 1 in 1meh

Go back to Potassium Binding Sites List in 1meh
Potassium binding site 1 out of 1 in the Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Imp and Moa 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 and Moa Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K900

b:29.5
occ:0.75
 OD2 A:ASP264 2.4 24.3 1.0
O A:PHE266 2.5 23.7 1.0
OD1 A:ASP264 2.9 23.8 1.0
CG A:ASP264 3.0 24.4 1.0
C A:PHE266 3.6 24.9 1.0
CB A:PHE266 3.7 24.8 1.0
CA A:PHE266 4.2 24.4 1.0
CG A:PHE266 4.5 25.1 1.0
CB A:ASP264 4.5 25.3 1.0
N A:PHE266 4.5 24.4 1.0
N A:SER267 4.7 25.5 1.0
CD2 A:PHE266 5.0 24.9 1.0

Reference:

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
Page generated: Mon Aug 12 04:57:38 2024

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