Magnesium in PDB 1mxb: S-Adenosylmethionine Synthetase with Adp

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

The structure of S-Adenosylmethionine Synthetase with Adp, PDB code: 1mxb 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 (%)	19.4 / 25.9

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

Potassium

(K)

2 atoms

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

Magnesium binding site 1 out of 2 in the S-Adenosylmethionine Synthetase with 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 Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg411 b:21.2 occ:1.00 O2B A:ADP385 2.1 42.9 1.0 OD2 A:ASP271 2.1 47.8 1.0 OD1 A:ASP271 2.2 28.4 1.0 O4 A:PO4384 2.2 34.3 1.0 CG A:ASP271 2.6 32.0 1.0 O2A A:ADP385 3.0 53.5 1.0 HZ2 A:LYS265 3.5 0.0 0.0 PB A:ADP385 3.6 41.2 1.0 P A:PO4384 3.8 22.5 1.0 OD2 A:ASP118 3.9 36.8 1.0 HZ3 A:LYS265 3.9 0.0 0.0 CB A:ASP271 4.1 16.6 1.0 PA A:ADP385 4.1 55.6 1.0 NZ A:LYS265 4.2 4.0 1.0 O3A A:ADP385 4.2 54.2 1.0 O3B A:ADP385 4.4 43.0 1.0 O3 A:PO4384 4.4 17.4 1.0 O1 A:PO4384 4.5 23.1 1.0 O2 A:PO4384 4.5 24.3 1.0 O1B A:ADP385 4.5 38.0 1.0 HZ1 A:LYS265 4.7 0.0 0.0 CA A:GLY260 4.7 5.8 1.0 O1A A:ADP385 4.9 66.3 1.0 O3' A:ADP385 5.0 0.2 1.0

Magnesium binding site 2 out of 2 in the S-Adenosylmethionine Synthetase with 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 Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg412 b:23.3 occ:1.00 O2 A:PO4384 2.0 24.3 1.0 O1A A:ADP385 2.1 66.3 1.0 O3B A:ADP385 2.9 43.0 1.0 P A:PO4384 3.5 22.5 1.0 PA A:ADP385 3.6 55.6 1.0 O3 A:PO4384 4.0 17.4 1.0 PB A:ADP385 4.2 41.2 1.0 O4 A:PO4384 4.3 34.3 1.0 O1 A:PO4384 4.3 23.1 1.0 O3A A:ADP385 4.3 54.2 1.0 O5' A:ADP385 4.4 74.0 1.0 O2A A:ADP385 4.5 53.5 1.0 OE2 A:GLU42 4.7 20.7 1.0 O2B A:ADP385 4.8 42.9 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