Magnesium in PDB 2x5z: Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose.

Enzymatic activity of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose.

All present enzymatic activity of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose.:
2.7.7.13;

Protein crystallography data

The structure of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose., PDB code: 2x5z was solved by M.C.Pelissier, S.Lesley, P.Kuhn, Y.Bourne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 2.70
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	84.227, 96.035, 217.122, 90.00, 90.00, 90.00
*R / R_free (%)*	19.111 / 24.415

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose. (pdb code 2x5z). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose., PDB code: 2x5z:

Magnesium binding site 1 out of 1 in 2x5z

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Magnesium Binding Sites List in 2x5z

Magnesium binding site 1 out of 1 in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose.

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gdp-Mannose. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg602 b:26.6 occ:1.00	O2A	A:GDD601	1.8	22.2	1.0
	O3B	A:GDD601	2.0	29.0	1.0
	OD1	A:ASP260	2.2	40.2	1.0
	O	A:HOH2023	2.3	23.0	1.0
	OD2	A:ASP109	2.3	39.3	1.0
	O	A:HOH2016	2.5	16.6	1.0
	PA	A:GDD601	3.2	25.0	1.0
	PB	A:GDD601	3.3	29.0	1.0
	CG	A:ASP109	3.3	37.5	1.0
	CG	A:ASP260	3.3	37.9	1.0
	O3A	A:GDD601	3.5	28.1	1.0
	OD1	A:ASP109	3.6	37.4	1.0
	O6A	A:GDD601	3.8	35.4	1.0
	OD2	A:ASP260	3.9	39.0	1.0
	O51	A:GDD601	4.2	27.5	1.0
	O5'	A:GDD601	4.3	25.3	1.0
	C5'	A:GDD601	4.3	24.6	1.0
	O1B	A:GDD601	4.4	30.4	1.0
	O2B	A:GDD601	4.4	32.7	1.0
	O1A	A:GDD601	4.4	23.4	1.0
	NZ	A:LYS25	4.5	35.5	1.0
	C61	A:GDD601	4.5	30.4	1.0
	C51	A:GDD601	4.5	29.8	1.0
	CB	A:ASP260	4.6	35.4	1.0
	CB	A:ASP109	4.7	38.7	1.0
	C11	A:GDD601	4.7	29.0	1.0

Reference:

M.C.Pelissier, S.Lesley, P.Kuhn, Y.Bourne. Structural Insights Into the Catalytic Mechanism of Bacterial Guanosine-Diphospho-D-Mannose Pyrophosphorylase and Its Regulation By Divalent Ions. J.Biol.Chem. V. 285 27468 2010.
ISSN: ISSN 0021-9258
PubMed: 20573954
DOI: 10.1074/JBC.M109.095182

Page generated: Wed Aug 14 06:59:45 2024

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