Magnesium in PDB 1g67: Thiamin Phosphate Synthase

All present enzymatic activity of Thiamin Phosphate Synthase:
2.5.1.3;

The structure of Thiamin Phosphate Synthase, PDB code: 1g67 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)	42.99 / 1.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.980, 76.980, 140.150, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 24

The binding sites of Magnesium atom in the Thiamin Phosphate Synthase (pdb code 1g67). 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: 1g67:
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:Mg2007 b:11.2 occ:1.00 O A:HOH2102 2.1 17.8 1.0 OD1 A:ASP93 2.1 15.3 1.0 O6 A:POP2003 2.1 12.1 1.0 O2 A:POP2003 2.2 14.4 0.6 O A:HOH2101 2.2 15.2 1.0 OD2 A:ASP112 2.2 13.3 1.0 O2 A:POP2003 2.3 14.4 0.4 CG A:ASP93 3.1 15.9 1.0 P1 A:POP2003 3.1 12.2 0.6 CG A:ASP112 3.2 16.2 1.0 P1 A:POP2003 3.2 12.2 0.4 OD2 A:ASP93 3.4 20.1 1.0 P2 A:POP2003 3.4 9.3 1.0 O A:POP2003 3.4 12.7 1.0 O1 A:POP2003 3.4 16.7 0.6 OD1 A:ASP112 3.4 18.4 1.0 N A:GLY109 3.8 11.4 1.0 O3 A:POP2003 3.9 14.2 0.4 NZ A:LYS61 4.0 16.6 1.0 O A:HOH2103 4.0 20.7 1.0 ND2 A:ASN92 4.1 15.2 1.0 OD1 A:ASN92 4.2 18.2 1.0 CA A:GLY109 4.3 13.0 1.0 O4 A:POP2003 4.3 10.9 1.0 O5 A:POP2003 4.3 10.2 1.0 CB A:ASP93 4.5 14.4 1.0 CG A:ASN92 4.5 12.2 1.0 O3 A:POP2003 4.5 14.2 0.6 CB A:ASP112 4.5 16.6 1.0 C A:ILE108 4.6 9.9 1.0 O1 A:POP2003 4.6 16.7 0.4 CA A:ILE108 4.8 9.6 1.0 CA A:ASP93 4.9 13.3 1.0 N A:ASP93 5.0 11.3 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:Mg2008 b:12.1 occ:1.00 O2 B:POP2004 2.1 5.8 0.6 OD1 B:ASP1093 2.1 16.0 1.0 O6 B:POP2004 2.1 12.4 1.0 O B:HOH2202 2.1 16.1 1.0 O3 B:POP2004 2.1 15.1 0.4 O B:HOH2201 2.2 13.1 1.0 OD2 B:ASP1112 2.2 12.2 1.0 CG B:ASP1093 3.1 16.1 1.0 P1 B:POP2004 3.1 16.9 0.6 CG B:ASP1112 3.2 14.9 1.0 P1 B:POP2004 3.2 16.5 0.4 P2 B:POP2004 3.4 12.6 1.0 OD2 B:ASP1093 3.4 18.4 1.0 O B:POP2004 3.4 12.8 1.0 OD1 B:ASP1112 3.4 16.9 1.0 O1 B:POP2004 3.5 18.3 0.6 N B:GLY1109 3.9 9.8 1.0 O B:HOH2203 3.9 18.0 1.0 O2 B:POP2004 4.0 5.4 0.4 NZ B:LYS1061 4.0 14.7 1.0 ND2 B:ASN1092 4.1 15.4 1.0 OD1 B:ASN1092 4.2 16.0 1.0 CA B:GLY1109 4.3 11.6 1.0 O B:HOH3200 4.3 40.0 1.0 O5 B:POP2004 4.3 12.6 1.0 O4 B:POP2004 4.3 11.2 1.0 O1 B:POP2004 4.4 17.9 0.4 CB B:ASP1093 4.4 13.8 1.0 O3 B:POP2004 4.5 15.6 0.6 CG B:ASN1092 4.5 10.8 1.0 CB B:ASP1112 4.5 14.2 1.0 C B:ILE1108 4.7 9.0 1.0 CA B:ASP1093 4.8 12.8 1.0 CA B:ILE1108 4.9 9.0 1.0 N B:ASP1093 5.0 11.6 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