Magnesium in PDB 1o92: Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue

All present enzymatic activity of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue:
2.5.1.6;

The structure of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue, PDB code: 1o92 was solved by B.Gonzalez, M.A.Pajares, J.A.Hermoso, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 3.19
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.140, 115.140, 160.450, 90.00, 90.00, 90.00
R / Rfree (%)	24.6 / 26.4

The structure of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Magnesium atom in the Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue (pdb code 1o92). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue, PDB code: 1o92:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1402 b:99.9 occ:1.00 CD1 B:ILE323 2.8 29.3 1.0 O2 A:PO41401 2.9 79.1 1.0 OD1 B:ASP135 3.1 26.0 1.0 OG A:SER248 3.6 35.6 1.0 O4 A:PO41401 3.9 54.3 1.0 P A:PO41401 4.0 83.7 1.0 CG1 B:ILE323 4.1 31.9 1.0 CG B:ASP135 4.3 24.1 1.0 CB A:PRO247 4.3 29.4 1.0 N B:ASP135 4.4 25.3 1.0 CA B:ASP135 4.5 26.6 1.0 O1 A:PO41401 4.5 73.9 1.0 CB B:ASP135 4.9 24.4 1.0 CB A:SER248 5.0 32.1 1.0

Magnesium binding site 2 out of 3 in the Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1403 b:71.8 occ:1.00 OXT A:AMB1398 2.4 87.3 1.0 OD2 A:ASP180 2.5 30.0 1.0 O A:AMB1398 2.6 82.6 1.0 C A:AMB1398 2.9 83.8 1.0 CD A:PRO31 3.1 12.0 1.0 CG A:ASP180 3.5 25.0 1.0 CG A:PRO31 3.6 10.2 1.0 O A:GLY255 3.7 53.6 1.0 OD1 A:ASP180 3.7 26.2 1.0 CD2 A:HIS30 4.2 11.1 1.0 CA A:AMB1398 4.3 79.6 1.0 NE2 A:HIS30 4.5 14.4 1.0 N A:PRO31 4.6 11.1 1.0 N A:GLY258 4.6 44.0 1.0 CA A:GLY258 4.6 43.3 1.0 CZ A:PHE251 4.7 37.5 1.0 CG A:HIS30 4.7 11.5 1.0 C A:GLY255 4.8 53.8 1.0 CA A:HIS30 4.8 9.2 1.0 CB A:ASP180 4.8 20.6 1.0 CB A:PRO31 4.9 9.6 1.0 N A:GLN257 4.9 51.2 1.0 CB A:AMB1398 5.0 69.4 1.0

Magnesium binding site 3 out of 3 in the Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1404 b:48.4 occ:1.00 OE2 A:GLU24 2.3 15.8 1.0 O3 A:PO41399 2.3 76.2 1.0 CE A:LYS266 2.9 20.4 1.0 NZ A:LYS266 3.0 23.9 1.0 CD A:GLU24 3.3 11.8 1.0 O B:HOH2088 3.3 28.3 1.0 P A:PO41399 3.5 80.1 1.0 OE1 A:GLU24 3.6 14.0 1.0 O1 A:PO41399 3.9 70.9 1.0 O4 A:PO41399 4.2 70.2 1.0 CD A:LYS266 4.2 12.4 1.0 O1 B:PO41400 4.4 72.5 1.0 CG A:GLU24 4.6 6.4 1.0 O4 B:PO41400 4.6 73.3 1.0 O B:HOH2065 4.7 36.4 1.0 CG1 A:VAL26 4.7 2.0 1.0 O2 A:PO41399 4.8 76.6 1.0 CG A:LYS266 4.8 8.9 1.0 CE A:LYS182 5.0 28.9 1.0

B.Gonzalez, M.A.Pajares, J.A.Hermoso, D.Guillerm, G.Guillerm, J.Sanz-Aparicio. Crystal Structures of Methionine Adenosyltransferase Complexed with Substrates and Products Reveal the Methionine-Atp Recognition and Give Insights Into the Catalytic Mechanism J.Mol.Biol. V. 331 407 2003.
ISSN: ISSN 0022-2836
PubMed: 12888348
DOI: 10.1016/S0022-2836(03)00728-9