Potassium in PDB 7loo: S-Adenosyl Methionine Transferase Cocrystallized with Atp

All present enzymatic activity of S-Adenosyl Methionine Transferase Cocrystallized with Atp:
2.5.1.6;

The structure of S-Adenosyl Methionine Transferase Cocrystallized with Atp, PDB code: 7loo was solved by C.J.Jackson, L.L.Tan, P.Laurino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.99 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.922, 117.78, 113.21, 90, 107.52, 90
R / Rfree (%)	17 / 20.7

The structure of S-Adenosyl Methionine Transferase Cocrystallized with Atp also contains other interesting chemical elements:

Magnesium

(Mg)

8 atoms

The binding sites of Potassium atom in the S-Adenosyl Methionine Transferase Cocrystallized with Atp (pdb code 7loo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the S-Adenosyl Methionine Transferase Cocrystallized with Atp, PDB code: 7loo:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the S-Adenosyl Methionine Transferase Cocrystallized with Atp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of S-Adenosyl Methionine Transferase Cocrystallized with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:K404 b:85.7 occ:1.00 O Q:HOH503 2.5 53.4 1.0 O6 A:POP401 2.6 24.6 1.0 OD1 A:ASP238 2.6 33.9 1.0 O4 A:POP401 2.7 31.6 1.0 O Q:HOH539 2.9 38.5 1.0 P2 A:POP401 3.2 26.4 1.0 OE2 Q:GLU42 3.3 52.4 1.0 O A:HOH515 3.4 20.6 1.0 CG A:ASP238 3.5 35.7 1.0 O Q:HOH643 3.6 44.3 1.0 OD2 A:ASP238 3.7 39.2 1.0 O A:HOH503 3.8 37.4 1.0 O A:CYS239 3.8 26.2 0.6 MG A:MG403 3.8 20.8 1.0 O A:HOH547 3.8 21.2 1.0 O A:CYS239 3.9 25.4 0.4 N A:SAM408 4.0 34.8 1.0 O A:POP401 4.0 28.1 1.0 CD Q:GLU42 4.4 47.0 1.0 N A:CYS239 4.5 24.0 0.6 O5 A:POP401 4.5 27.9 1.0 NH2 A:ARG244 4.5 24.8 1.0 N A:CYS239 4.5 24.1 0.4 CB A:CYS239 4.6 26.9 0.4 OE2 Q:GLU55 4.7 42.1 1.0 CG Q:GLU42 4.7 37.7 1.0 C A:CYS239 4.7 24.6 0.6 C A:CYS239 4.8 24.7 0.4 O1 A:POP401 4.8 18.1 1.0 CB A:ASP238 4.9 33.1 1.0 CG A:SAM408 4.9 43.3 1.0 CB A:CYS239 4.9 27.3 0.6 CA A:CYS239 4.9 24.1 0.4 CA A:CYS239 5.0 23.4 0.6 O2 A:PO4402 5.0 44.9 1.0

Potassium binding site 2 out of 4 in the S-Adenosyl Methionine Transferase Cocrystallized with Atp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of S-Adenosyl Methionine Transferase Cocrystallized with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:K405 b:109.5 occ:1.00 NH1 A:ARG293 3.1 84.6 1.0 OH A:TYR125 3.2 41.8 1.0 O Q:HOH724 3.8 64.7 1.0 CE1 A:PHE315 3.9 39.2 1.0 CZ A:TYR125 4.1 36.3 1.0 CZ A:PHE315 4.1 35.6 1.0 CD1 A:PHE315 4.2 41.9 1.0 CE1 A:TYR125 4.2 36.7 1.0 O A:MET254 4.3 34.7 1.0 CZ A:ARG293 4.3 85.5 1.0 CE2 A:PHE315 4.5 31.3 1.0 CD A:ARG293 4.5 64.3 1.0 CG A:PHE315 4.6 40.0 1.0 CD2 A:PHE315 4.7 36.9 1.0 SD A:MET254 4.7 45.3 1.0 O A:HOH559 4.7 51.8 1.0 CG A:MET254 4.8 37.1 1.0 NH1 Q:ARG256 4.8 48.7 1.0 NE A:ARG293 4.9 78.0 1.0

Potassium binding site 3 out of 4 in the S-Adenosyl Methionine Transferase Cocrystallized with Atp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of S-Adenosyl Methionine Transferase Cocrystallized with Atp within 5.0Å range: probe atom residue distance (Å) B Occ Q:K405 b:76.4 occ:1.00 O5 Q:POP401 2.6 23.1 1.0 OD1 Q:ASP238 2.7 36.7 1.0 O4 Q:POP401 3.0 31.6 1.0 O A:HOH512 3.0 45.5 1.0 OE2 A:GLU42 3.1 51.7 1.0 O Q:HOH530 3.2 21.4 1.0 P2 Q:POP401 3.3 25.9 1.0 CG Q:ASP238 3.5 33.2 1.0 O A:HOH578 3.5 48.8 1.0 O Q:CYS239 3.5 27.5 0.6 OD2 Q:ASP238 3.6 38.8 1.0 O Q:HOH547 3.6 21.3 1.0 O Q:CYS239 3.7 27.5 0.4 MG Q:MG412 3.7 22.6 1.0 O Q:HOH505 4.0 34.3 1.0 N Q:SAM410 4.1 32.3 1.0 O Q:POP401 4.1 26.6 1.0 CD A:GLU42 4.2 44.4 1.0 N Q:CYS239 4.3 28.3 0.4 N Q:CYS239 4.3 27.4 0.6 CB Q:CYS239 4.4 30.4 0.4 NH2 Q:ARG244 4.5 26.0 1.0 C Q:CYS239 4.5 27.6 0.6 C Q:CYS239 4.5 27.7 0.4 CG A:GLU42 4.6 36.9 1.0 CA Q:CYS239 4.6 28.8 0.4 O6 Q:POP401 4.7 25.9 1.0 CB Q:CYS239 4.7 30.7 0.6 OE2 A:GLU55 4.7 45.6 1.0 CA Q:CYS239 4.7 28.7 0.6 CG Q:SAM410 4.8 45.0 1.0 CB Q:ASP238 4.8 28.5 1.0 O1 Q:POP401 4.8 20.4 1.0 C Q:ASP238 4.9 30.7 1.0

Potassium binding site 4 out of 4 in the S-Adenosyl Methionine Transferase Cocrystallized with Atp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of S-Adenosyl Methionine Transferase Cocrystallized with Atp within 5.0Å range: probe atom residue distance (Å) B Occ Q:K406 b:116.6 occ:1.00 NH1 Q:ARG293 2.8 48.5 0.5 O Q:HOH624 2.8 52.6 1.0 OH Q:TYR125 3.4 40.9 1.0 O A:HOH727 3.9 69.9 1.0 CD Q:ARG293 3.9 46.5 0.5 CZ Q:ARG293 4.0 51.0 0.5 CD Q:ARG293 4.1 46.0 0.6 CE1 Q:PHE315 4.2 37.9 1.0 CD1 Q:PHE315 4.3 38.4 1.0 CZ Q:TYR125 4.3 36.0 1.0 CZ Q:PHE315 4.3 34.6 1.0 NE Q:ARG293 4.4 50.8 0.5 CG Q:PHE315 4.5 39.4 1.0 CE1 Q:TYR125 4.5 37.4 1.0 CE2 Q:PHE315 4.5 35.5 1.0 O Q:MET254 4.6 34.8 1.0 CD2 Q:PHE315 4.6 37.9 1.0 SD Q:MET254 4.7 43.6 1.0 CG Q:ARG293 4.7 43.0 0.5 NH1 A:ARG256 5.0 46.4 1.0

C.J.Jackson, P.L.Laurino. Protein and Substrate Flexibility Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferase To Be Published.