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Potassium in PDB 7rxx: Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site

Enzymatic activity of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site

All present enzymatic activity of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site:
2.5.1.6;

Protein crystallography data

The structure of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site, PDB code: 7rxx 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) 19.88 / 1.25
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.224, 94.121, 117.159, 90, 90, 90
R / Rfree (%) 12.9 / 14.1

Other elements in 7rxx:

The structure of Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Sodium (Na) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site (pdb code 7rxx). 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 Two Sulfate in the Active Site, PDB code: 7rxx:

Potassium binding site 1 out of 1 in 7rxx

Go back to Potassium Binding Sites List in 7rxx
Potassium binding site 1 out of 1 in the Human Methionine Adenosyltransferase 2A Bound to Methylthioadenosine and Two Sulfate in the Active Site


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 Two Sulfate in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K409

b:10.0
occ:0.66
 O A:HOH538 2.0 10.4 0.5
OD1 A:ASP258 2.7 14.5 0.8
O A:HOH531 2.8 14.5 1.0
O A:ALA259 2.9 8.3 1.0
O A:HOH538 3.3 10.4 0.5
O A:HOH548 3.4 11.7 1.0
HB3 A:ALA259 3.4 9.8 1.0
O A:HOH751 3.6 22.4 1.0
CG A:ASP258 3.6 9.7 0.7
H A:ALA259 3.8 8.5 1.0
C A:ALA259 3.9 6.5 1.0
MG A:MG407 3.9 6.7 0.7
OD2 A:ASP258 3.9 9.0 0.5
N A:ALA259 4.0 7.0 1.0
O A:HOH501 4.1 12.9 0.6
HH22 A:ARG264 4.2 13.7 1.0
CB A:ALA259 4.3 8.2 1.0
CA A:ALA259 4.3 6.3 1.0
N A:ALA401 4.5 18.7 1.0
HD11 A:LEU261 4.5 14.1 0.4
HD12 A:LEU261 4.6 14.1 0.4
C A:ASP258 4.6 8.1 1.0
NH2 A:ARG264 4.7 11.4 1.0
HA A:ASP258 4.7 9.6 1.0
HB1 A:ALA259 4.8 9.8 1.0
HD13 A:LEU261 4.8 14.1 0.4
HH21 A:ARG264 4.8 13.7 1.0
CB A:ASP258 4.9 9.6 1.0
HA2 A:GLY260 4.9 8.0 1.0
HB2 A:ALA259 4.9 9.8 1.0
CD1 A:LEU261 4.9 11.8 0.4
CA A:ASP258 5.0 8.0 1.0

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: Mon Aug 12 20:57:51 2024

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