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Magnesium in PDB 1n0h: Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl

Enzymatic activity of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl

All present enzymatic activity of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl:
4.1.3.18;

Protein crystallography data

The structure of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl, PDB code: 1n0h was solved by S.S.Pang, L.W.Guddat, R.G.Duggleby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.70 / 2.80
Space group P 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 153.976, 153.976, 178.298, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.5

Other elements in 1n0h:

The structure of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl also contains other interesting chemical elements:

Potassium (K) 2 atoms
Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl (pdb code 1n0h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl, PDB code: 1n0h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1n0h

Go back to Magnesium Binding Sites List in 1n0h
Magnesium binding site 1 out of 2 in the Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg699

b:2.6
occ:1.00
 OD1 A:ASN577 2.1 17.3 1.0
OD1 A:ASP550 2.1 17.4 1.0
O3B A:AYD700 2.1 16.2 1.0
O A:GLU579 2.2 24.2 1.0
O A:HOH771 2.2 4.6 1.0
O1A A:AYD700 2.2 19.4 1.0
CG A:ASN577 3.0 16.7 1.0
CG A:ASP550 3.2 15.9 1.0
PB A:AYD700 3.3 16.9 1.0
PA A:AYD700 3.3 18.9 1.0
O3A A:AYD700 3.3 18.7 1.0
C A:GLU579 3.4 24.5 1.0
ND2 A:ASN577 3.4 15.9 1.0
OD2 A:ASP550 3.6 16.7 1.0
O2B A:AYD700 3.8 16.9 1.0
N A:ASP550 3.9 16.0 1.0
O7 A:AYD700 4.0 23.0 1.0
N A:GLY581 4.0 25.8 1.0
N A:GLU579 4.0 23.5 1.0
N A:ALA551 4.2 17.5 1.0
CA A:GLU579 4.3 23.3 1.0
N A:GLN580 4.3 26.8 1.0
O2A A:AYD700 4.3 20.0 1.0
CG A:GLU579 4.3 23.8 1.0
N A:ASN577 4.4 18.4 1.0
CA A:GLN580 4.4 27.3 1.0
CB A:ASN577 4.4 18.1 1.0
CB A:ASP550 4.4 15.6 1.0
O1B A:AYD700 4.5 17.0 1.0
O A:LEU575 4.5 16.9 1.0
CA A:ASP550 4.6 16.0 1.0
C A:GLY549 4.6 16.3 1.0
CA A:GLY549 4.6 15.8 1.0
N A:GLU578 4.7 21.2 1.0
C A:GLN580 4.7 27.2 1.0
CA A:ASN577 4.8 19.0 1.0
CB A:ALA551 4.8 16.4 1.0
C A:ASN577 4.8 20.6 1.0
CA A:GLY581 4.8 25.1 1.0
C A:ASP550 5.0 16.7 1.0
CB A:GLU579 5.0 22.9 1.0

Magnesium binding site 2 out of 2 in 1n0h

Go back to Magnesium Binding Sites List in 1n0h
Magnesium binding site 2 out of 2 in the Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with A Sulfonylurea Herbicide, Chlorimuron Ethyl within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1699

b:25.9
occ:1.00
 O1A B:TPP1702 2.1 32.4 1.0
O B:GLU579 2.1 42.6 1.0
OD1 B:ASN577 2.1 36.3 1.0
OD1 B:ASP550 2.2 21.0 1.0
O B:HOH1032 2.3 23.2 1.0
O3B B:TPP1702 2.4 35.8 1.0
CG B:ASN577 3.1 35.9 1.0
O3A B:TPP1702 3.1 34.4 1.0
PA B:TPP1702 3.2 32.2 1.0
CG B:ASP550 3.2 18.7 1.0
C B:GLU579 3.3 43.6 1.0
PB B:TPP1702 3.4 33.5 1.0
ND2 B:ASN577 3.4 36.2 1.0
OD2 B:ASP550 3.6 18.7 1.0
N B:GLY581 4.0 40.1 1.0
N B:GLU579 4.0 43.2 1.0
N B:ASP550 4.0 17.0 1.0
O2A B:TPP1702 4.0 33.5 1.0
O2B B:TPP1702 4.0 35.6 1.0
N B:ALA551 4.2 16.5 1.0
CA B:GLU579 4.3 43.9 1.0
N B:GLN580 4.3 44.1 1.0
O7 B:TPP1702 4.3 35.5 1.0
CA B:GLN580 4.4 43.8 1.0
CB B:ASP550 4.5 16.4 1.0
CG B:GLU579 4.5 47.4 1.0
N B:ASN577 4.5 31.0 1.0
CB B:ASN577 4.5 34.2 1.0
O1B B:TPP1702 4.5 35.7 1.0
O B:LEU575 4.6 23.3 1.0
CA B:ASP550 4.7 17.1 1.0
C B:GLY549 4.7 19.2 1.0
CA B:GLY549 4.7 18.5 1.0
C B:GLN580 4.7 42.7 1.0
CB B:ALA551 4.8 15.0 1.0
N B:GLU578 4.8 39.7 1.0
CA B:GLY581 4.8 38.6 1.0
CA B:ASN577 4.9 34.4 1.0
C B:ASN577 4.9 37.1 1.0
C B:ASP550 5.0 16.6 1.0

Reference:

S.S.Pang, L.W.Guddat, R.G.Duggleby. Molecular Basis of Sulfonylurea Herbicide Inhibition of Acetohydroxyacid Synthase J.Biol.Chem. V. 278 7639 2003.
ISSN: ISSN 0021-9258
PubMed: 14557277
DOI: 10.1074/JBC.M211648200
Page generated: Tue Aug 13 09:17:34 2024

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