Magnesium in PDB 1mxc: S-Adenosylmethionine Synthetase with 8-Br-Adp

All present enzymatic activity of S-Adenosylmethionine Synthetase with 8-Br-Adp:
2.5.1.6;

The structure of S-Adenosylmethionine Synthetase with 8-Br-Adp, PDB code: 1mxc 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 / 3.00
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 (%)	18.7 / 25.9

The structure of S-Adenosylmethionine Synthetase with 8-Br-Adp also contains other interesting chemical elements:

Potassium	(K)	2 atoms
Bromine	(Br)	1 atom

The binding sites of Magnesium atom in the S-Adenosylmethionine Synthetase with 8-Br-Adp (pdb code 1mxc). 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 8-Br-Adp, PDB code: 1mxc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the S-Adenosylmethionine Synthetase with 8-Br-Adp


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 8-Br-Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg411 b:20.0 occ:1.00 O2B A:ABP385 2.1 37.9 1.0 O4 A:PO4384 2.1 30.4 1.0 OD2 A:ASP271 2.1 40.7 1.0 OD1 A:ASP271 2.3 23.3 1.0 CG A:ASP271 2.7 26.1 1.0 O2A A:ABP385 2.9 34.3 1.0 HZ2 A:LYS265 3.4 17.6 0.0 PB A:ABP385 3.6 40.4 1.0 P A:PO4384 3.6 27.4 1.0 HZ3 A:LYS265 3.8 17.6 0.0 OD2 A:ASP118 4.0 38.3 1.0 PA A:ABP385 4.0 46.6 1.0 NZ A:LYS265 4.1 5.7 1.0 O3A A:ABP385 4.2 46.4 1.0 CB A:ASP271 4.2 12.9 1.0 O3 A:PO4384 4.2 15.3 1.0 O3B A:ABP385 4.3 41.5 1.0 O1 A:PO4384 4.4 20.5 1.0 O2 A:PO4384 4.4 23.6 1.0 O1B A:ABP385 4.6 34.5 1.0 HZ1 A:LYS265 4.7 17.6 0.0 O1A A:ABP385 4.7 49.8 1.0 CA A:GLY260 4.8 7.8 1.0 O3' A:ABP385 4.9 0.3 1.0 H A:ALA261 5.0 17.6 0.0

Magnesium binding site 2 out of 2 in the S-Adenosylmethionine Synthetase with 8-Br-Adp


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 8-Br-Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg412 b:41.4 occ:1.00 O2 A:PO4384 2.0 23.6 1.0 O1A A:ABP385 2.1 49.8 1.0 O3B A:ABP385 2.8 41.5 1.0 P A:PO4384 3.5 27.4 1.0 PA A:ABP385 3.6 46.6 1.0 O3 A:PO4384 4.0 15.3 1.0 PB A:ABP385 4.1 40.4 1.0 O3A A:ABP385 4.2 46.4 1.0 O4 A:PO4384 4.3 30.4 1.0 O1 A:PO4384 4.4 20.5 1.0 O5' A:ABP385 4.4 62.6 1.0 O2A A:ABP385 4.5 34.3 1.0 OE2 A:GLU42 4.6 26.2 1.0 O2B A:ABP385 4.8 37.9 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