Magnesium in PDB 4rsr: Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone

The structure of Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone, PDB code: 4rsr was solved by C.Packianathan, K.Marapakala, A.A.Ajees, P.Kandavelu, B.P.Rosen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.70 / 2.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.156, 46.406, 100.255, 90.00, 114.07, 90.00
R / Rfree (%)	17.3 / 22.4

The structure of Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone also contains other interesting chemical elements:

Arsenic	(As)	1 atom
Calcium	(Ca)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone (pdb code 4rsr). 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 Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone, PDB code: 4rsr:

Magnesium binding site 1 out of 1 in the Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Arsm Arsenic(III) S-Adenosylmethionine Methyltransferase with Trivalent Phenyl Arsencial Derivative-Roxarsone within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:29.3 occ:1.00 OE1 A:GLN292 2.7 18.8 1.0 N A:TYR290 2.8 16.1 1.0 O A:VAL320 2.8 20.3 1.0 N A:GLN292 3.1 21.7 1.0 CB A:GLN292 3.1 18.0 1.0 CA A:TYR290 3.4 18.1 1.0 N A:GLY291 3.4 19.6 1.0 C A:TYR290 3.4 19.8 1.0 CG A:GLN292 3.5 19.4 1.0 CD A:GLN292 3.5 20.3 1.0 CB A:TYR290 3.6 17.1 1.0 N A:ARG322 3.6 15.3 1.0 CA A:GLN292 3.7 19.1 1.0 C A:ASP321 3.8 15.4 1.0 OD1 A:ASP289 3.8 18.2 1.0 C A:ASP289 3.9 15.7 1.0 C A:VAL320 3.9 19.8 1.0 CA A:ASP321 4.0 17.2 1.0 CA A:ARG322 4.1 15.0 1.0 O A:TYR290 4.1 18.4 1.0 C A:GLY291 4.1 23.3 1.0 CA A:ASP289 4.2 15.9 1.0 O A:GLU288 4.2 15.1 1.0 NH2 A:ARG319 4.2 21.8 1.0 O A:ASP321 4.3 17.1 1.0 CB A:ARG322 4.3 14.8 1.0 CA A:GLY291 4.3 19.6 1.0 O A:GLN292 4.4 17.2 1.0 C A:GLN292 4.5 18.8 1.0 N A:ASP321 4.5 17.4 1.0 CG A:TYR290 4.8 18.5 1.0 NE2 A:GLN292 4.8 16.7 1.0 CG A:ASP289 4.9 19.5 1.0 CD1 A:TYR290 4.9 18.1 1.0 CG2 A:VAL320 4.9 17.0 1.0

C.Packianathan, K.Marapakala, A.A.Ajees, P.Kandavelu, B.P.Rosen. A Disulfide Bond Cascade Mechanism For As(III) S-Adenosylmethionine Methyltransferases To Be Published.