Magnesium in PDB 1r6w: Crystal Structure of the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc

The structure of Crystal Structure of the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc, PDB code: 1r6w was solved by V.A.Klenchin, E.A.Taylor Ringia, J.A.Gerlt, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.62
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	72.200, 82.900, 56.200, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20

The binding sites of Magnesium atom in the Crystal Structure of the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc (pdb code 1r6w). 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 of the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc, PDB code: 1r6w:

Magnesium binding site 1 out of 1 in the Crystal Structure of the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc


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 the K133R Mutant of O-Succinylbenzoate Synthase (Osbs) From Escherichia Coli. Complex with Shchc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg736 b:14.4 occ:1.00 OE2 A:GLU190 2.0 14.4 1.0 OD1 A:ASP213 2.0 15.2 1.0 O A:HOH1073 2.1 13.8 1.0 OD2 A:ASP161 2.1 16.1 1.0 O2 A:164735 2.1 18.6 1.0 O1 A:164735 2.1 17.5 1.0 C7 A:164735 2.5 23.4 1.0 CG A:ASP213 3.1 16.6 1.0 CG A:ASP161 3.1 16.4 1.0 CD A:GLU190 3.1 16.5 1.0 OD1 A:ASP161 3.4 14.1 1.0 CB A:ASP213 3.6 11.8 1.0 OE1 A:GLU190 3.9 14.4 1.0 NZ A:LYS131 3.9 27.9 1.0 NZ A:LYS235 4.0 27.4 1.0 ND2 A:ASN163 4.0 20.0 1.0 CB A:GLU190 4.1 12.8 1.0 C2 A:164735 4.1 23.4 1.0 OE2 A:GLU214 4.1 15.5 1.0 OD2 A:ASP213 4.1 15.0 1.0 CG A:GLU190 4.2 12.9 1.0 O A:HOH872 4.2 27.8 1.0 CB A:ASP161 4.4 13.5 1.0 CE A:LYS235 4.6 16.6 1.0 C3 A:164735 4.7 27.1 1.0 CD A:GLU214 4.8 21.5 1.0 CE A:LYS131 4.9 24.0 1.0 O A:HOH938 4.9 35.9 1.0 OE1 A:GLU214 4.9 24.4 1.0 CG A:ASN163 4.9 19.0 1.0 C1 A:164735 4.9 24.0 1.0 O3 A:164735 5.0 25.9 1.0

V.A.Klenchin, E.A.Taylor Ringia, J.A.Gerlt, I.Rayment. Evolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed By O-Succinylbenzoate Synthase From Escherichia Coli Biochemistry V. 42 14427 2003.
ISSN: ISSN 0006-2960
PubMed: 14661953
DOI: 10.1021/BI035545V