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Magnesium in PDB 7u25: Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium

Enzymatic activity of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium:
2.2.1.6;

Protein crystallography data

The structure of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium, PDB code: 7u25 was solved by L.W.Guddat, Y.Cheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.43 / 3.19
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 179.952, 179.952, 185.472, 90, 90, 120
R / Rfree (%) 17.4 / 19.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium (pdb code 7u25). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium, PDB code: 7u25:

Magnesium binding site 1 out of 1 in 7u25

Go back to Magnesium Binding Sites List in 7u25
Magnesium binding site 1 out of 1 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium


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 Arabidopsis Thaliana Acetohydroxyacid Synthase W574L Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:66.1
occ:1.00
 O13 A:TZD704 2.0 71.6 0.9
O23 A:TZD704 2.1 74.9 0.9
O A:HIS567 2.2 71.1 1.0
OD1 A:ASN565 2.2 83.5 1.0
OD1 A:ASP538 2.4 83.6 1.0
P2 A:TZD704 3.1 67.6 0.9
CG A:ASN565 3.1 72.9 1.0
P1 A:TZD704 3.1 59.3 0.9
O11 A:TZD704 3.4 78.9 0.9
ND2 A:ASN565 3.4 76.9 1.0
C A:HIS567 3.4 69.6 1.0
O21 A:TZD704 3.5 69.8 0.9
CG A:ASP538 3.5 79.3 1.0
N A:GLY569 3.8 79.0 1.0
O5G A:TZD704 3.9 63.2 0.9
OD2 A:ASP538 4.0 89.0 1.0
N A:ASP538 4.0 88.7 1.0
N A:HIS567 4.2 76.7 1.0
N A:LEU568 4.2 68.9 1.0
CA A:LEU568 4.3 64.5 1.0
O12 A:TZD704 4.3 57.4 0.9
CA A:HIS567 4.4 69.2 1.0
O22 A:TZD704 4.4 62.0 0.9
N A:GLY539 4.4 63.6 1.0
CB A:ASN565 4.5 74.7 1.0
N A:ASN565 4.6 77.6 1.0
C A:LEU568 4.6 76.7 1.0
CA A:GLY537 4.6 67.7 1.0
CA A:GLY569 4.6 70.6 1.0
C A:GLY537 4.7 74.1 1.0
CB A:ASP538 4.7 68.6 1.0
O A:LEU563 4.7 70.2 1.0
CA A:ASP538 4.8 71.8 1.0
CA A:ASN565 4.9 65.5 1.0
CD1 A:LEU588 4.9 70.9 1.0
N A:GLN566 5.0 67.9 1.0
C A:ASN565 5.0 75.3 1.0

Reference:

T.Lonhienne, Y.Cheng, M.D.Garcia, S.H.Hu, Y.S.Low, G.Schenk, C.M.Williams, L.W.Guddat. Structural Basis of Resistance to Herbicides That Target Acetohydroxyacid Synthase. Nat Commun V. 13 3368 2022.
ISSN: ESSN 2041-1723
PubMed: 35690625
DOI: 10.1038/S41467-022-31023-X
Page generated: Thu Oct 3 09:41:37 2024

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