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Potassium in PDB 7rxw: Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp)

Enzymatic activity of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp)

All present enzymatic activity of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp):
2.5.1.6;

Protein crystallography data

The structure of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp), PDB code: 7rxw was solved by E.Fedorov, C.N.Niland, V.L.Schramm, A.Ghosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.89 / 1.07
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.322, 94.069, 117.344, 90, 90, 90
R / Rfree (%) 12.8 / 13.8

Other elements in 7rxw:

The structure of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp) (pdb code 7rxw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp), PDB code: 7rxw:

Potassium binding site 1 out of 1 in 7rxw

Go back to Potassium Binding Sites List in 7rxw
Potassium binding site 1 out of 1 in the Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Inhibitor Imido-Diphosphate (Pnp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K407

b:16.2
occ:0.39
 OD1 A:ASP258 2.8 12.4 0.7
O A:ALA259 2.9 11.2 1.0
O6 A:2PN403 3.0 18.1 0.6
O A:HOH526 3.4 16.9 1.0
O A:HOH520 3.4 19.4 1.0
HB3 A:ALA259 3.4 12.9 1.0
CG A:ASP258 3.6 8.4 0.6
H A:ALA259 3.7 11.0 1.0
OD2 A:ASP258 3.8 10.2 0.6
C A:ALA259 3.8 8.3 1.0
N A:ALA259 3.9 9.1 1.0
MG A:MG405 4.0 11.6 0.5
O5 A:2PN403 4.0 17.8 0.5
HH22 A:ARG264 4.1 16.2 1.0
P2 A:2PN403 4.1 13.7 0.4
O A:HOH502 4.1 31.2 1.0
CA A:ALA259 4.2 8.6 1.0
CB A:ALA259 4.2 10.8 1.0
N A:ALA402 4.4 9.8 0.5
C A:ASP258 4.5 9.1 1.0
NH2 A:ARG264 4.6 13.5 1.0
HA A:ASP258 4.6 11.6 1.0
HD12 A:LEU261 4.6 14.5 0.4
HD11 A:LEU261 4.6 14.5 0.4
HH21 A:ARG264 4.7 16.2 1.0
HD13 A:LEU261 4.7 14.5 0.4
HB1 A:ALA259 4.8 12.9 1.0
CB A:ASP258 4.8 10.8 1.0
HB2 A:ALA259 4.8 12.9 1.0
HA2 A:GLY260 4.8 10.0 1.0
CA A:ASP258 4.9 9.6 1.0
CD1 A:LEU261 4.9 12.1 0.4
N1 A:2PN403 4.9 17.0 0.6

Reference:

A.Ghosh, C.N.Niland, S.M.Cahill, N.M.Karadkhelkar, V.L.Schramm. Mechanism of Triphosphate Hydrolysis By Human MAT2A at 1.07 Angstrom Resolution. J.Am.Chem.Soc. 2021.
ISSN: ESSN 1520-5126
PubMed: 34668717
DOI: 10.1021/JACS.1C09328
Page generated: Sat Aug 9 14:50:45 2025

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