Magnesium in PDB 1fhv: Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb

The structure of Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb, PDB code: 1fhv was solved by I.Rayment, T.B.Thompson, J.A.Gerlt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.77
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.800, 83.000, 57.400, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.4

The binding sites of Magnesium atom in the Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb (pdb code 1fhv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb, PDB code: 1fhv:

Magnesium binding site 1 out of 1 in the Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of O-Succinylbenzoate Synthase From E. Coli Complexed with Mg and Osb within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg790 b:17.5 occ:1.00 OE2 A:GLU190 2.0 17.8 1.0 OD1 A:ASP213 2.1 11.6 1.0 O A:HOH592 2.1 13.2 1.0 OD2 A:ASP161 2.2 15.4 1.0 O1 A:OSB789 2.2 24.0 1.0 O A:HOH674 2.3 25.0 1.0 CG A:ASP213 3.1 18.8 1.0 CG A:ASP161 3.1 18.9 1.0 CD A:GLU190 3.2 18.5 1.0 C7 A:OSB789 3.3 0.0 1.0 OD1 A:ASP161 3.5 15.3 1.0 CB A:ASP213 3.6 10.3 1.0 OE1 A:GLU190 3.7 14.6 1.0 O2 A:OSB789 3.9 49.5 1.0 NZ A:LYS235 4.0 11.8 0.8 O3 A:OSB789 4.0 72.2 1.0 NZ A:LYS235 4.0 1.0 0.2 O A:HOH758 4.1 25.9 1.0 O A:HOH673 4.1 13.2 1.0 OD1 A:ASN163 4.2 28.3 1.0 OD2 A:ASP213 4.2 11.8 1.0 CB A:GLU190 4.3 7.2 1.0 NZ A:LYS131 4.3 16.0 0.5 CG A:GLU190 4.3 8.8 1.0 CB A:ASP161 4.4 11.3 1.0 C2 A:OSB789 4.5 36.8 1.0 O A:HOH785 4.7 51.6 1.0 C8 A:OSB789 4.7 20.9 1.0 O5 A:OSB789 4.8 35.8 1.0 CE A:LYS235 4.9 1.6 0.2

T.B.Thompson, J.B.Garrett, E.A.Taylor, R.Meganathan, J.A.Gerlt, I.Rayment. Evolution of Enzymatic Activity in the Enolase Superfamily: Structure of O-Succinylbenzoate Synthase From Escherichia Coli in Complex with MG2+ and O-Succinylbenzoate. Biochemistry V. 39 10662 2000.
ISSN: ISSN 0006-2960
PubMed: 10978150
DOI: 10.1021/BI000855O