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Potassium in PDB 1xrb: S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse)

Enzymatic activity of S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse)

All present enzymatic activity of S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse):
2.5.1.6;

Protein crystallography data

The structure of S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse), PDB code: 1xrb was solved by F.Takusagawa, S.Kamitori, S.Misaki, G.D.Markham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 3.00
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 (%) 18.8 / 26.5

Other elements in 1xrb:

The structure of S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse) (pdb code 1xrb). 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 (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse), PDB code: 1xrb:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1xrb

Go back to Potassium Binding Sites List in 1xrb
Potassium binding site 1 out of 2 in the S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse)


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 (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K413

b:52.9
occ:1.00
OE2 A:GLU42 2.8 33.5 1.0
OE1 A:GLU42 2.9 21.2 1.0
O A:SER263 3.1 24.4 1.0
CD A:GLU42 3.1 22.1 1.0
CE A:LYS265 3.5 29.0 1.0
HG1 A:THR242 3.7 17.6 0.0
CG A:LYS265 3.8 15.3 1.0
OG1 A:THR242 3.8 16.6 1.0
CD A:LYS265 4.1 17.9 1.0
C A:SER263 4.3 21.2 1.0
CG A:GLU42 4.3 14.2 1.0
O2 A:PO4385 4.4 85.7 1.0
NZ A:LYS265 4.5 34.1 1.0
HZ3 A:LYS265 4.5 17.6 0.0
CB A:ALA261 4.6 15.8 1.0
O4 A:PO4385 4.6 80.0 1.0
O A:CYS41 4.6 23.1 1.0
HZ1 A:LYS265 4.7 17.6 0.0
C A:GLY264 4.8 24.3 1.0
CA A:GLY264 4.8 20.2 1.0
H A:CYS41 4.8 17.6 0.0
O A:GLY264 4.9 27.4 1.0

Potassium binding site 2 out of 2 in 1xrb

Go back to Potassium Binding Sites List in 1xrb
Potassium binding site 2 out of 2 in the S-Adenosylmethionine Synthetase (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse)


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 (Mat, Atp: L-Methionine S- Adenosyltransferase, E.C.2.5.1.6) in Which Met Residues Are Replaced with Selenomethionine Residues (Mse) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K414

b:68.5
occ:0.50
O A:GLY243 2.6 16.9 1.0
CD1 A:ILE246 3.3 41.6 1.0
C A:GLY243 3.8 18.0 1.0
CA A:ARG244 4.1 18.8 1.0
CG1 A:ILE246 4.1 26.1 1.0
CD A:ARG244 4.1 10.9 1.0
CB A:ILE246 4.1 19.8 1.0
O A:ARG244 4.2 28.3 1.0
H A:ILE246 4.3 17.6 0.0
N A:ARG244 4.4 17.6 1.0
C A:ARG244 4.5 22.4 1.0
CG2 A:ILE246 4.5 6.1 1.0
CG A:ARG244 4.7 8.2 1.0
O A:GLY259 4.8 32.8 1.0
CA A:GLY243 4.9 18.2 1.0
CB A:ARG244 4.9 15.1 1.0

Reference:

F.Takusagawa, S.Kamitori, S.Misaki, G.D.Markham. Crystal Structure of S-Adenosylmethionine Synthetase. J.Biol.Chem. V. 271 136 1996.
ISSN: ISSN 0021-9258
PubMed: 8550549
DOI: 10.1074/JBC.271.1.136
Page generated: Mon Aug 12 05:47:48 2024

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