Magnesium in PDB 1g69: Thiamin Phosphate Synthase

All present enzymatic activity of Thiamin Phosphate Synthase:
2.5.1.3;

The structure of Thiamin Phosphate Synthase, PDB code: 1g69 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)	19.91 / 1.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.480, 76.480, 139.880, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 23.2

The binding sites of Magnesium atom in the Thiamin Phosphate Synthase (pdb code 1g69). 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: 1g69:
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:24.2 occ:1.00 O2 A:POP2003 2.3 32.0 1.0 O A:HOH2102 2.3 23.9 1.0 OD2 A:ASP112 2.3 34.0 1.0 OD1 A:ASP93 2.4 14.4 1.0 O5 A:POP2003 2.4 27.8 1.0 O A:HOH2101 2.5 33.6 1.0 OD2 A:ASP93 3.1 17.3 1.0 P1 A:POP2003 3.1 32.8 1.0 CG A:ASP93 3.1 16.0 1.0 CG A:ASP112 3.3 36.0 1.0 O A:POP2003 3.4 28.4 1.0 NZ A:LYS61 3.4 19.2 1.0 O1 A:POP2003 3.5 32.7 1.0 P2 A:POP2003 3.5 21.7 1.0 OD1 A:ASP112 3.6 36.7 1.0 N A:GLY109 3.8 14.0 1.0 CA A:GLY109 4.0 15.3 1.0 ND2 A:ASN92 4.3 10.7 1.0 O6 A:POP2003 4.3 27.3 1.0 OD1 A:ASN92 4.4 15.5 1.0 C A:ILE108 4.5 11.3 1.0 O3 A:POP2003 4.6 30.5 1.0 CB A:ASP93 4.6 13.4 1.0 O4 A:POP2003 4.6 26.4 1.0 CB A:ASP112 4.7 35.2 1.0 CG A:ASN92 4.7 11.0 1.0 CE A:LYS61 4.8 20.2 1.0 CA A:ILE108 4.9 10.4 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:24.8 occ:1.00 O5 B:POP2004 2.0 31.9 1.0 O B:HOH2201 2.0 26.8 1.0 O B:HOH2202 2.2 29.1 1.0 OD1 B:ASP1093 2.4 20.2 1.0 OD2 B:ASP1112 2.5 33.1 1.0 O2 B:POP2004 2.7 34.0 1.0 OD2 B:ASP1093 2.9 25.3 1.0 CG B:ASP1093 3.0 20.3 1.0 P1 B:POP2004 3.2 34.5 1.0 P2 B:POP2004 3.2 32.0 1.0 O1 B:POP2004 3.2 33.3 1.0 O B:POP2004 3.4 32.9 1.0 CG B:ASP1112 3.4 32.8 1.0 NZ B:LYS1061 3.6 28.6 1.0 OD1 B:ASP1112 3.6 33.6 1.0 N B:GLY1109 3.8 12.6 1.0 OD1 B:ASN1092 4.1 17.7 1.0 ND2 B:ASN1092 4.1 18.5 1.0 CA B:GLY1109 4.1 13.8 1.0 O4 B:POP2004 4.2 31.2 1.0 O6 B:POP2004 4.2 31.7 1.0 CB B:ASP1093 4.4 17.1 1.0 CG B:ASN1092 4.5 14.4 1.0 C B:ILE1108 4.6 9.6 1.0 O3 B:POP2004 4.8 32.9 1.0 CA B:ILE1108 4.8 9.2 1.0 CB B:ASP1112 4.8 31.6 1.0 CE B:LYS1061 4.9 26.9 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