Potassium 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:

Magnesium

(Mg)

2 atoms

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

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of S-Adenosylmethionine Synthetase with Ppi within 5.0Å range: probe atom residue distance (Å) B Occ A:K413 b:71.1 occ:1.00 OE1 A:GLU42 2.5 28.9 1.0 O A:SER263 2.5 9.5 1.0 CD A:GLU42 3.2 18.8 1.0 OE2 A:GLU42 3.3 24.4 1.0 HG1 A:THR242 3.3 24.0 0.0 CG A:LYS265 3.6 4.0 1.0 OG1 A:THR242 3.7 10.2 1.0 C A:SER263 3.7 6.6 1.0 CE A:LYS265 3.7 9.0 1.0 CD A:LYS265 4.2 4.0 1.0 CA A:GLY264 4.2 8.7 1.0 C A:GLY264 4.3 14.4 1.0 O A:CYS41 4.3 13.1 1.0 N A:GLY264 4.4 4.9 1.0 N A:LYS265 4.4 11.4 1.0 CG A:GLU42 4.5 15.6 1.0 H A:CYS41 4.5 24.0 0.0 H A:LYS265 4.6 24.0 0.0 CB A:ALA261 4.6 9.5 1.0 O A:GLY264 4.6 14.7 1.0 C A:CYS41 4.8 13.3 1.0 CB A:LYS265 4.8 5.2 1.0 O A:PHE262 4.9 21.1 1.0 NZ A:LYS265 4.9 15.9 1.0 CA A:SER263 4.9 9.3 1.0 N A:CYS41 4.9 15.7 1.0 HZ3 A:LYS265 5.0 24.0 0.0

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of S-Adenosylmethionine Synthetase with Ppi within 5.0Å range: probe atom residue distance (Å) B Occ A:K414 b:69.0 occ:0.50 O A:GLY243 2.6 17.3 1.0 CG2 A:ILE246 3.4 29.4 1.0 C A:GLY243 3.8 12.0 1.0 CB A:ILE246 4.0 13.7 1.0 CD1 A:ILE246 4.0 6.6 1.0 CA A:ARG244 4.2 14.5 1.0 CD A:ARG244 4.3 12.0 1.0 O A:ARG244 4.4 20.8 1.0 CG1 A:ILE246 4.4 10.1 1.0 N A:ARG244 4.5 12.7 1.0 H A:ILE246 4.7 24.0 0.0 C A:ARG244 4.7 17.9 1.0 O A:GLY259 4.8 24.6 1.0 CG A:ARG244 4.9 4.0 1.0 CA A:GLY243 4.9 8.8 1.0 HE A:ARG244 5.0 24.0 0.0

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