Magnesium in PDB 1g4s: Thiamin Phosphate Synthase

All present enzymatic activity of Thiamin Phosphate Synthase:
2.5.1.3;

The structure of Thiamin Phosphate Synthase, PDB code: 1g4s was solved by D.H.Peapus, H.-J.Chiu, N.Campobasso, J.J.Reddick, T.P.Begley, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.96 / 1.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.990, 76.990, 139.850, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.9

The binding sites of Magnesium atom in the Thiamin Phosphate Synthase (pdb code 1g4s). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Thiamin Phosphate Synthase, PDB code: 1g4s:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Thiamin Phosphate Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thiamin Phosphate Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2005 b:15.9 occ:1.00 O2 A:POP2003 2.0 19.3 1.0 O A:HOH2102 2.1 15.4 1.0 O5 A:POP2003 2.1 15.4 1.0 OD2 A:ASP112 2.2 16.6 1.0 O A:HOH2101 2.2 19.4 1.0 OD1 A:ASP93 2.3 23.1 1.0 CG A:ASP112 3.1 20.8 1.0 CG A:ASP93 3.2 24.7 1.0 P1 A:POP2003 3.3 20.6 1.0 P2 A:POP2003 3.3 15.0 1.0 OD1 A:ASP112 3.4 19.9 1.0 OD2 A:ASP93 3.4 27.9 1.0 O A:POP2003 3.5 17.0 1.0 N A:GLY109 3.8 14.2 1.0 O A:HOH2103 3.9 25.9 1.0 NZ A:LYS61 4.1 18.8 1.0 O A:HOH2116 4.1 18.3 1.0 ND2 A:ASN92 4.1 15.2 1.0 O3 A:POP2003 4.2 21.9 1.0 OD1 A:ASN92 4.2 17.9 1.0 CA A:GLY109 4.2 15.1 1.0 O4 A:POP2003 4.3 12.8 1.0 O6 A:POP2003 4.3 15.9 1.0 O1 A:POP2003 4.4 17.5 1.0 CB A:ASP112 4.5 20.2 1.0 O A:HOH2117 4.5 55.5 1.0 CG A:ASN92 4.6 15.4 1.0 CB A:ASP93 4.6 20.6 1.0 C A:ILE108 4.6 12.6 1.0 CA A:ILE108 4.9 11.9 1.0

Magnesium binding site 2 out of 2 in the Thiamin Phosphate Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Thiamin Phosphate Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2006 b:15.5 occ:1.00 O2 B:POP2004 2.0 16.2 1.0 O5 B:POP2004 2.0 15.5 1.0 OD1 B:ASP1093 2.1 18.4 1.0 O B:HOH2202 2.2 16.4 1.0 O B:HOH3032 2.2 14.1 1.0 OD2 B:ASP1112 2.3 18.8 1.0 CG B:ASP1093 3.1 20.5 1.0 CG B:ASP1112 3.2 20.1 1.0 P2 B:POP2004 3.2 13.7 1.0 P1 B:POP2004 3.3 22.4 1.0 OD2 B:ASP1093 3.4 25.1 1.0 O B:POP2004 3.4 16.3 1.0 OD1 B:ASP1112 3.5 22.1 1.0 N B:GLY1109 3.9 12.2 1.0 O3 B:POP2004 3.9 23.7 1.0 NZ B:LYS1061 4.0 17.4 1.0 O B:HOH2216 4.1 19.5 1.0 O B:HOH2203 4.1 21.5 1.0 OD1 B:ASN1092 4.2 16.0 1.0 O6 B:POP2004 4.2 15.6 1.0 O4 B:POP2004 4.2 15.7 1.0 ND2 B:ASN1092 4.2 14.8 1.0 CA B:GLY1109 4.3 13.2 1.0 O1 B:POP2004 4.3 20.0 1.0 CB B:ASP1093 4.5 18.4 1.0 CB B:ASP1112 4.6 19.4 1.0 CG B:ASN1092 4.6 13.0 1.0 C B:ILE1108 4.7 11.6 1.0 CA B:ASP1093 4.9 15.7 1.0

D.H.Peapus, H.J.Chiu, N.Campobasso, J.J.Reddick, T.P.Begley, S.E.Ealick. Structural Characterization of the Enzyme-Substrate, Enzyme-Intermediate, and Enzyme-Product Complexes of Thiamin Phosphate Synthase. Biochemistry V. 40 10103 2001.
ISSN: ISSN 0006-2960
PubMed: 11513589
DOI: 10.1021/BI0104726