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Magnesium in PDB 1o93: Methionine Adenosyltransferase Complexed with Atp and A L-Methionine Analogue

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

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

Protein crystallography data

The structure of Methionine Adenosyltransferase Complexed with Atp and A L-Methionine Analogue, PDB code: 1o93 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 / 3.49
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 115.200, 115.200, 160.890, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 27.3

Other elements in 1o93:

The structure of Methionine Adenosyltransferase Complexed with Atp and 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 Atp and A L-Methionine Analogue (pdb code 1o93). 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 Atp and A L-Methionine Analogue, PDB code: 1o93:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1o93

Go back to Magnesium Binding Sites List in 1o93
Magnesium binding site 1 out of 3 in the Methionine Adenosyltransferase Complexed with Atp 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 Atp and A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1401

b:20.0
occ:1.00
O2 A:PO41400 2.3 20.0 1.0
OG A:SER248 2.8 38.2 1.0
OD1 B:ASP135 3.3 26.3 1.0
P A:PO41400 3.6 20.0 1.0
O3 A:PO41400 3.9 20.0 1.0
CB A:SER248 4.2 35.1 1.0
O4 A:PO41400 4.2 20.0 1.0
CD1 B:ILE323 4.5 37.5 1.0
CG B:ASP135 4.5 27.2 1.0
O A:LIS1398 4.6 20.0 1.0
CB A:PRO247 4.8 29.6 1.0
N A:SER248 4.8 32.0 1.0
O1 A:PO41400 4.8 20.0 1.0

Magnesium binding site 2 out of 3 in 1o93

Go back to Magnesium Binding Sites List in 1o93
Magnesium binding site 2 out of 3 in the Methionine Adenosyltransferase Complexed with Atp 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 Atp and A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1402

b:20.0
occ:1.00
OXT A:LIS1398 2.6 20.0 1.0
O3G B:ATP1397 2.6 20.0 1.0
C A:LIS1398 3.2 20.0 1.0
O A:LIS1398 3.2 20.0 1.0
O3B B:ATP1397 3.2 20.0 1.0
CD A:LYS182 3.3 39.7 1.0
CB A:LYS182 3.3 24.9 1.0
PG B:ATP1397 3.4 20.0 1.0
CG A:LYS182 3.8 30.8 1.0
O2B B:ATP1397 4.0 20.0 1.0
PB B:ATP1397 4.1 20.0 1.0
O2G B:ATP1397 4.1 20.0 1.0
CA A:LIS1398 4.5 20.0 1.0
CE A:LYS182 4.6 43.8 1.0
CD2 A:HIS30 4.6 12.8 1.0
CA A:LYS182 4.6 18.4 1.0
O1G B:ATP1397 4.6 20.0 1.0
O3 A:PO41400 4.8 20.0 1.0
NE2 A:HIS30 4.8 14.2 1.0
NZ A:LYS182 4.9 48.6 1.0
N A:LYS182 4.9 17.9 1.0
N A:LIS1398 4.9 20.0 1.0

Magnesium binding site 3 out of 3 in 1o93

Go back to Magnesium Binding Sites List in 1o93
Magnesium binding site 3 out of 3 in the Methionine Adenosyltransferase Complexed with Atp 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 Atp and A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1403

b:20.0
occ:1.00
O A:HOH2001 1.8 49.3 1.0
NZ A:LYS266 2.9 17.7 1.0
OE2 A:GLU24 3.1 11.8 1.0
CE A:LYS266 3.3 10.6 1.0
O A:HOH2003 3.6 60.8 1.0
O3G B:ATP1397 3.7 20.0 1.0
O1G B:ATP1397 3.8 20.0 1.0
CD A:GLU24 3.8 10.7 1.0
OE1 A:GLU24 3.9 9.9 1.0
O2G B:ATP1397 3.9 20.0 1.0
PG B:ATP1397 4.0 20.0 1.0
O1 B:PO41399 4.1 20.0 1.0
CE A:LYS182 4.5 43.8 1.0
NE2 A:HIS30 4.7 14.2 1.0
CD A:LYS266 4.7 2.0 1.0
O2 B:PO41399 4.8 20.0 1.0
O4 B:PO41399 4.8 20.0 1.0
P B:PO41399 4.8 20.0 1.0
NZ A:LYS182 4.8 48.6 1.0
CG1 A:VAL26 4.9 2.0 1.0
O A:HOH2052 4.9 7.4 1.0
CD A:LYS182 5.0 39.7 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 10:34:32 2024

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