Magnesium in PDB 2egh: Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin

All present enzymatic activity of Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin:
1.1.1.267;

The structure of Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin, PDB code: 2egh was solved by S.Yajima, K.Hara, D.Iino, Y.Sasaki, T.Kuzuyama, H.Seto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.21 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	180.590, 59.115, 87.050, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 22.5

The binding sites of Magnesium atom in the Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin (pdb code 2egh). 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 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin, PDB code: 2egh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin


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 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg900 b:65.6 occ:1.00 OD1 A:ASP149 2.0 43.8 1.0 OE2 A:GLU230 2.1 28.5 1.0 O A:HOH3151 2.2 41.4 1.0 O2 A:FOM1001 2.3 75.9 1.0 O1 A:FOM1001 2.4 77.3 1.0 OE2 A:GLU151 2.6 28.4 1.0 C1 A:FOM1001 2.9 77.1 1.0 CG A:ASP149 3.0 43.1 1.0 N1 A:FOM1001 3.0 77.6 1.0 OD2 A:ASP149 3.3 44.2 1.0 CD A:GLU230 3.3 24.1 1.0 NZ A:LYS124 3.3 43.7 1.0 CD A:GLU151 3.6 28.1 1.0 OE1 A:GLU151 3.8 29.6 1.0 OE1 A:GLU230 4.1 24.3 1.0 OD1 A:ASN226 4.3 40.5 1.0 CG A:GLU230 4.3 23.2 1.0 CB A:ASP149 4.4 36.4 1.0 C5N A:NDP3001 4.4 84.9 1.0 C2 A:FOM1001 4.4 77.0 1.0 ND2 A:ASN226 4.5 37.9 1.0 CE A:LYS124 4.6 44.0 1.0 N A:SER150 4.7 29.0 1.0 C4N A:NDP3001 4.8 83.5 1.0 CG A:ASN226 4.8 37.3 1.0 CA A:ASP149 4.9 32.0 1.0 CG A:GLU151 4.9 26.4 1.0 N A:GLU151 5.0 24.1 1.0 C3 A:FOM1001 5.0 76.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin


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 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase Complexed with A Magnesium Ion, Nadph and Fosmidomycin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg901 b:53.4 occ:1.00 O1 B:FOM2001 2.1 75.9 1.0 OE1 B:GLU230 2.1 23.6 1.0 O2 B:FOM2001 2.1 73.9 1.0 OD1 B:ASP149 2.2 44.4 1.0 O B:HOH3153 2.3 43.9 1.0 OE2 B:GLU151 2.4 29.4 1.0 C1 B:FOM2001 2.6 75.5 1.0 N1 B:FOM2001 2.7 75.6 1.0 CG B:ASP149 3.2 43.7 1.0 CD B:GLU230 3.2 26.2 1.0 CD B:GLU151 3.3 30.6 1.0 OD2 B:ASP149 3.5 46.2 1.0 OE1 B:GLU151 3.5 32.0 1.0 NZ B:LYS124 3.8 50.8 1.0 OE2 B:GLU230 3.8 25.9 1.0 ND2 B:ASN226 4.1 37.4 1.0 C2 B:FOM2001 4.2 75.2 1.0 CG B:GLU230 4.3 24.3 1.0 N B:SER150 4.5 29.5 1.0 CB B:ASP149 4.5 37.5 1.0 C5N B:NDP3002 4.6 79.4 1.0 OD1 B:ASN226 4.6 35.9 1.0 CG B:GLU151 4.7 27.3 1.0 N B:GLU151 4.7 27.5 1.0 C4N B:NDP3002 4.8 78.6 1.0 CG B:ASN226 4.8 34.2 1.0 CA B:ASP149 4.9 33.7 1.0 CB B:SER150 4.9 30.1 1.0 CE B:LYS124 4.9 48.0 1.0 C3 B:FOM2001 4.9 75.3 1.0 C B:ASP149 5.0 32.0 1.0

S.Yajima, K.Hara, D.Iino, Y.Sasaki, T.Kuzuyama, K.Ohsawa, H.Seto. Structure of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase in A Quaternary Complex with A Magnesium Ion, Nadph and the Antimalarial Drug Fosmidomycin Acta Crystallogr.,Sect.F V. 63 466 2007.
ISSN: ESSN 1744-3091
PubMed: 17554164
DOI: 10.1107/S1744309107024475