Magnesium in PDB 2x65: Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate.

All present enzymatic activity of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate.:
2.7.7.13;

The structure of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate., PDB code: 2x65 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)	65.21 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.933, 91.738, 69.730, 90.00, 110.75, 90.00
R / Rfree (%)	18.7 / 23.01

The binding sites of Magnesium atom in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate. (pdb code 2x65). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate., PDB code: 2x65:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate.


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 Mannose-1-Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:47.3 occ:1.00 O A:HOH2062 1.9 30.2 1.0 O1P A:M1P600 2.0 46.2 1.0 O A:HOH2061 2.1 31.0 1.0 O A:HOH2064 2.2 26.7 1.0 O A:HOH2023 2.3 27.7 1.0 O A:HOH2063 2.4 25.7 1.0 P A:M1P600 3.2 47.0 1.0 O3P A:M1P600 3.3 44.9 1.0 O A:HOH2065 3.8 28.5 1.0 O5 A:M1P600 4.0 41.6 1.0 C1 A:M1P600 4.1 44.4 1.0 O1 A:M1P600 4.1 45.3 1.0 O A:HOH2022 4.2 22.9 1.0 O A:HOH2041 4.3 28.7 1.0 O2P A:M1P600 4.3 47.0 1.0 NE2 A:HIS110 4.5 33.7 1.0 O A:HOH2043 4.6 30.6 1.0 O6 A:M1P600 4.7 41.2 1.0 OD1 A:ASP109 4.8 35.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Mannose-1-Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:55.9 occ:1.00 O B:HOH2031 2.1 40.8 1.0 O B:HOH2089 2.1 47.6 1.0 O B:HOH2087 2.1 48.4 1.0 O3P B:M1P600 2.2 49.4 1.0 O B:HOH2088 2.2 46.4 1.0 P B:M1P600 3.6 50.5 1.0 O B:HOH2001 3.9 46.1 1.0 NE2 B:HIS110 3.9 26.6 1.0 O5 B:M1P600 3.9 40.3 1.0 O2P B:M1P600 4.1 52.6 1.0 C1 B:M1P600 4.2 42.0 1.0 O1 B:M1P600 4.5 44.5 1.0 OD1 B:ASP109 4.5 35.5 1.0 O1P B:M1P600 4.6 51.5 1.0 OD2 B:ASP109 4.6 37.9 1.0 O6 B:M1P600 4.7 39.6 1.0 CE1 B:HIS110 4.8 30.4 1.0 O B:HOH2006 4.8 48.6 1.0 CD2 B:HIS110 4.9 25.4 1.0 O B:HOH2004 4.9 43.3 1.0 CB B:PRO107 5.0 31.3 1.0

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