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Magnesium in PDB 1o90: Methionine Adenosyltransferase Complexed with A L-Methionine Analogue

Enzymatic activity of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue

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

Protein crystallography data

The structure of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1o90 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 / 3.10
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 114.890, 114.890, 161.080, 90.00, 90.00, 90.00
R / Rfree (%) 24.4 / 28.6

Other elements in 1o90:

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

Potassium (K) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue (pdb code 1o90). 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 A L-Methionine Analogue, PDB code: 1o90:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1o90

Go back to Magnesium Binding Sites List in 1o90
Magnesium binding site 1 out of 3 in the Methionine Adenosyltransferase Complexed with 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 A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1401

b:66.7
occ:1.00
O2 A:PO41400 2.9 90.0 1.0
CD1 B:ILE323 2.9 36.6 1.0
OG A:SER248 3.1 46.5 1.0
O4 A:PO41400 3.5 91.1 1.0
P A:PO41400 3.5 89.4 1.0
OD1 B:ASP135 3.7 32.7 1.0
CB A:PRO247 3.8 31.8 1.0
O3 A:PO41400 3.9 89.5 1.0
CG1 B:ILE323 4.3 37.9 1.0
N A:SER248 4.4 39.9 1.0
CB A:SER248 4.5 43.4 1.0
CG A:PRO247 4.6 32.0 1.0
C A:PRO247 4.7 38.2 1.0
CA A:SER248 4.8 40.5 1.0
CG B:ASP135 4.8 31.9 1.0
CA A:PRO247 4.9 33.8 1.0
N B:ASP135 4.9 32.3 1.0
CA B:ASP135 5.0 35.5 1.0

Magnesium binding site 2 out of 3 in 1o90

Go back to Magnesium Binding Sites List in 1o90
Magnesium binding site 2 out of 3 in the Methionine Adenosyltransferase Complexed with 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 A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1402

b:37.9
occ:1.00
O A:LIS1397 2.9 80.6 1.0
N A:LIS1397 3.0 77.2 1.0
OD2 A:ASP180 3.0 26.0 1.0
C A:LIS1397 3.7 79.6 1.0
CA A:LIS1397 3.7 78.5 1.0
CG A:ASP180 4.1 24.1 1.0
CD A:PRO31 4.2 22.1 1.0
O A:GLY255 4.3 57.8 1.0
OD1 A:ASP180 4.4 25.6 1.0
CZ A:PHE251 4.4 29.7 1.0
CA A:GLY258 4.5 50.0 1.0
CG A:PRO31 4.6 21.5 1.0
CD2 A:HIS30 4.7 17.0 1.0
N A:GLY258 4.7 50.6 1.0
NE2 A:HIS30 4.9 19.8 1.0
OXT A:LIS1397 4.9 78.6 1.0

Magnesium binding site 3 out of 3 in 1o90

Go back to Magnesium Binding Sites List in 1o90
Magnesium binding site 3 out of 3 in the Methionine Adenosyltransferase Complexed with 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 A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1403

b:47.2
occ:1.00
OE2 A:GLU24 2.4 27.1 1.0
O2 A:PO41398 2.8 85.7 1.0
CE A:LYS266 3.0 26.2 1.0
O4 A:PO41398 3.1 86.3 1.0
NZ A:LYS266 3.2 33.5 1.0
CD A:GLU24 3.2 21.7 1.0
P A:PO41398 3.3 84.2 1.0
OE1 A:GLU24 3.5 22.8 1.0
O1 A:PO41398 3.7 85.5 1.0
O B:HOH2084 3.7 44.5 1.0
CG1 A:VAL26 4.1 8.7 1.0
CD A:LYS266 4.4 17.9 1.0
CG A:GLU24 4.4 16.7 1.0
CE A:LYS182 4.5 42.8 1.0
O1 B:PO41399 4.6 75.2 1.0
NE2 A:HIS30 4.7 19.8 1.0
O B:HOH2061 4.8 21.1 1.0
CG A:LYS266 4.9 13.2 1.0
O3 A:PO41398 4.9 85.5 1.0
CD A:LYS182 5.0 41.0 1.0

Reference:

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
Page generated: Tue Aug 13 10:33:58 2024

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