Magnesium in PDB 1mxa: S-Adenosylmethionine Synthetase with Ppi

All present enzymatic activity of S-Adenosylmethionine Synthetase with Ppi:
2.5.1.6;

The structure of S-Adenosylmethionine Synthetase with Ppi, PDB code: 1mxa was solved by F.Takusagawa, S.Kamitori, G.D.Markham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.80
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	128.900, 128.900, 139.800, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 25.7

The structure of S-Adenosylmethionine Synthetase with Ppi also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Magnesium atom in the S-Adenosylmethionine Synthetase with Ppi (pdb code 1mxa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the S-Adenosylmethionine Synthetase with Ppi, PDB code: 1mxa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the S-Adenosylmethionine Synthetase with Ppi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of S-Adenosylmethionine Synthetase with Ppi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg411 b:28.1 occ:1.00 O6 A:POP385 2.0 44.1 1.0 O2 A:POP385 2.0 31.4 1.0 O4 A:PO4384 2.1 44.1 1.0 OD2 A:ASP271 2.2 46.2 1.0 OD1 A:ASP271 2.7 26.7 1.0 CG A:ASP271 2.9 30.4 1.0 P1 A:POP385 3.2 31.5 1.0 HZ2 A:LYS265 3.2 24.0 0.0 P2 A:POP385 3.3 38.5 1.0 O A:POP385 3.5 40.2 1.0 P A:PO4384 3.6 31.8 1.0 HZ3 A:LYS265 3.6 24.0 0.0 NZ A:LYS265 3.9 15.9 1.0 O3 A:POP385 3.9 34.5 1.0 O2 A:PO4384 4.1 37.7 1.0 O4 A:POP385 4.1 51.4 1.0 O3 A:PO4384 4.2 35.1 1.0 O5 A:POP385 4.3 43.9 1.0 O1 A:POP385 4.3 28.1 1.0 CB A:ASP271 4.3 20.2 1.0 HZ1 A:LYS265 4.4 24.0 0.0 OD2 A:ASP118 4.4 27.9 1.0 O1 A:PO4384 4.5 39.5 1.0 CA A:GLY260 4.8 6.6 1.0 MG A:MG412 4.9 47.1 1.0

Magnesium binding site 2 out of 2 in the S-Adenosylmethionine Synthetase with Ppi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of S-Adenosylmethionine Synthetase with Ppi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg412 b:47.1 occ:1.00 O4 A:POP385 1.9 51.4 1.0 O3 A:POP385 2.0 34.5 1.0 O2 A:PO4384 2.0 37.7 1.0 P2 A:POP385 3.2 38.5 1.0 P1 A:POP385 3.2 31.5 1.0 P A:PO4384 3.4 31.8 1.0 O A:POP385 3.4 40.2 1.0 O6 A:POP385 3.9 44.1 1.0 O4 A:PO4384 3.9 44.1 1.0 O3 A:PO4384 4.0 35.1 1.0 O2 A:POP385 4.1 31.4 1.0 O1 A:POP385 4.3 28.1 1.0 O5 A:POP385 4.3 43.9 1.0 O1 A:PO4384 4.4 39.5 1.0 HZ3 A:LYS265 4.8 24.0 0.0 MG A:MG411 4.9 28.1 1.0 OE2 A:GLU42 4.9 24.4 1.0

F.Takusagawa, S.Kamitori, G.D.Markham. Structure and Function of S-Adenosylmethionine Synthetase: Crystal Structures of S-Adenosylmethionine Synthetase with Adp, Bradp, and Ppi at 28 Angstroms Resolution. Biochemistry V. 35 2586 1996.
ISSN: ISSN 0006-2960
PubMed: 8611562
DOI: 10.1021/BI952604Z