Potassium in PDB 1mew: Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Xmp and Nad Bound

Enzymatic activity of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Xmp and Nad Bound

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

Protein crystallography data

The structure of Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Xmp and Nad Bound, PDB code: 1mew 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)*	29.61 / 2.15
*Space group*	P 4 3 2
*Cell size a, b, c (Å), α, β, γ (°)*	153.827, 153.827, 153.827, 90.00, 90.00, 90.00
*R / R_free (%)*	22.4 / 24.6

Potassium Binding Sites:

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

Potassium binding site 1 out of 1 in 1mew

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Potassium Binding Sites List in 1mew

Potassium binding site 1 out of 1 in the Inosine Monophosphate Dehydrogenase (Impdh) From Tritrichomonas Foetus with Xmp and Nad 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 Xmp and Nad Bound within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K900 b:33.2 occ:0.75	OD2	A:ASP264	2.5	28.6	1.0
	O	A:PHE266	2.7	26.9	1.0
	OD1	A:ASP264	2.9	28.2	1.0
	CG	A:ASP264	3.1	29.1	1.0
	C	A:PHE266	3.6	27.3	1.0
	CB	A:PHE266	3.7	26.3	1.0
	CA	A:PHE266	4.2	26.5	1.0
	O	A:HOH1136	4.4	55.2	1.0
	CG	A:PHE266	4.5	26.3	1.0
	CB	A:ASP264	4.6	29.2	1.0
	N	A:PHE266	4.6	26.3	1.0
	N	A:SER267	4.7	28.4	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: Sun Dec 13 22:51:49 2020

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