Magnesium in PDB 2x60: Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gtp.

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

The structure of Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gtp., PDB code: 2x60 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)	67.57 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.926, 79.567, 70.952, 90.00, 107.75, 90.00
R / Rfree (%)	20.737 / 26.697

The binding sites of Magnesium atom in the Crystal Structure of T. Maritima Gdp-Mannose Pyrophosphorylase in Complex with Gtp. (pdb code 2x60). 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 Gtp., PDB code: 2x60:
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 Gtp.


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 Gtp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:39.6 occ:1.00 O2G A:GTP601 2.3 44.4 1.0 O2B A:GTP601 2.3 45.6 1.0 O1A A:GTP601 2.5 50.3 1.0 PG A:GTP601 3.5 45.0 1.0 PB A:GTP601 3.5 43.1 1.0 PA A:GTP601 3.7 46.8 1.0 O1G A:GTP601 3.8 45.9 1.0 O3B A:GTP601 3.9 45.0 1.0 O3A A:GTP601 4.0 45.9 1.0 NH2 A:ARG326 4.4 55.4 1.0 O2A A:GTP601 4.4 50.0 1.0 NH2 A:ARG14 4.4 42.4 1.0 ND2 A:ASN85 4.5 50.3 1.0 C8 A:GTP601 4.6 50.0 1.0 OD1 A:ASN85 4.6 53.0 1.0 O1B A:GTP601 4.8 43.8 1.0 O3G A:GTP601 4.8 42.2 1.0 NE A:ARG326 4.9 57.6 1.0 CG A:ASN85 4.9 52.1 1.0 N7 A:GTP601 4.9 50.7 1.0 O5' A:GTP601 4.9 46.0 1.0

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


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 Gtp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:43.2 occ:1.00 O3G B:GTP601 2.0 53.5 1.0 O2A B:GTP601 2.2 60.3 1.0 O1B B:GTP601 2.5 54.7 1.0 PG B:GTP601 3.4 55.8 1.0 PA B:GTP601 3.5 56.6 1.0 PB B:GTP601 3.6 57.0 1.0 O3A B:GTP601 3.9 56.5 1.0 O3B B:GTP601 3.9 57.4 1.0 NH2 B:ARG14 4.1 53.6 1.0 O1G B:GTP601 4.1 57.9 1.0 NH2 B:ARG326 4.1 66.0 1.0 OD1 B:ASN85 4.2 82.7 1.0 O5' B:GTP601 4.4 59.4 1.0 O2G B:GTP601 4.5 55.8 1.0 C8 B:GTP601 4.5 71.1 1.0 O1A B:GTP601 4.6 58.2 1.0 N7 B:GTP601 4.8 71.9 1.0 O2B B:GTP601 5.0 55.3 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