Magnesium in PDB 1g4p: Thiamin Phosphate Synthase

All present enzymatic activity of Thiamin Phosphate Synthase:
2.5.1.3;

The structure of Thiamin Phosphate Synthase, PDB code: 1g4p 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)	53.94 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.280, 76.280, 139.590, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 29.5

The structure of Thiamin Phosphate Synthase also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Magnesium atom in the Thiamin Phosphate Synthase (pdb code 1g4p). 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: 1g4p:
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:Mg2003 b:11.8 occ:1.00 O2 A:FQP2001 2.0 10.9 1.0 O A:HOH2102 2.1 5.3 1.0 O A:HOH2101 2.2 8.6 1.0 OD1 A:ASP93 2.2 6.8 1.0 O5 A:FQP2001 2.3 12.0 1.0 OD2 A:ASP112 2.4 26.4 1.0 P1 A:FQP2001 3.0 6.9 1.0 O A:FQP2001 3.0 9.1 1.0 CG A:ASP93 3.2 3.6 1.0 P2 A:FQP2001 3.3 10.4 1.0 CG A:ASP112 3.3 26.0 1.0 OD1 A:ASP112 3.4 26.6 1.0 OD2 A:ASP93 3.5 2.4 1.0 O1 A:FQP2001 3.7 6.0 1.0 N A:GLY109 3.9 10.6 1.0 O A:HOH2103 4.0 21.7 1.0 NZ A:LYS61 4.1 11.8 1.0 OD1 A:ASN92 4.1 2.4 1.0 ND2 A:ASN92 4.1 2.4 1.0 O6 A:FQP2001 4.2 11.0 1.0 O3 A:FQP2001 4.2 11.9 1.0 O4 A:FQP2001 4.3 9.2 1.0 CA A:GLY109 4.4 12.9 1.0 CG A:ASN92 4.5 5.1 1.0 CB A:ASP93 4.6 3.7 1.0 C A:ILE108 4.6 9.5 1.0 CB A:ASP112 4.7 25.4 1.0 CA A:ILE108 4.9 7.9 1.0 CA A:ASP93 4.9 4.8 1.0 N A:ASP93 5.0 5.0 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:Mg2004 b:6.1 occ:1.00 O B:HOH2201 2.1 12.4 1.0 OD1 B:ASP1093 2.2 4.2 1.0 O B:HOH2202 2.2 6.7 1.0 O2 B:FQP2002 2.2 7.6 1.0 O5 B:FQP2002 2.2 10.2 1.0 OD1 B:ASP1112 2.3 14.1 1.0 CG B:ASP1093 3.2 5.2 1.0 P1 B:FQP2002 3.2 7.7 1.0 O B:FQP2002 3.2 7.0 1.0 CG B:ASP1112 3.3 12.0 1.0 P2 B:FQP2002 3.3 9.0 1.0 OD2 B:ASP1093 3.5 8.1 1.0 OD2 B:ASP1112 3.5 12.3 1.0 O1 B:FQP2002 3.8 7.4 1.0 N B:GLY1109 3.8 6.6 1.0 OD1 B:ASN1092 4.0 2.4 1.0 O4 B:FQP2002 4.1 7.6 1.0 NZ B:LYS1061 4.1 22.8 1.0 ND2 B:ASN1092 4.1 5.6 1.0 CA B:GLY1109 4.4 5.5 1.0 O6 B:FQP2002 4.4 8.4 1.0 O3 B:FQP2002 4.4 9.0 1.0 CG B:ASN1092 4.5 3.5 1.0 C B:ILE1108 4.5 6.9 1.0 CB B:ASP1093 4.5 3.6 1.0 CB B:ASP1112 4.6 10.1 1.0 CA B:ILE1108 4.6 4.4 1.0 CA B:ASP1093 4.8 3.5 1.0 N B:ASP1093 4.9 2.4 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