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Magnesium in PDB 7tzz: Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium

Enzymatic activity of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium:
2.2.1.6;

Protein crystallography data

The structure of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium, PDB code: 7tzz 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) 44.89 / 2.59
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 179.558, 179.558, 184.839, 90, 90, 120
R / Rfree (%) 15.5 / 16.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium (pdb code 7tzz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium, PDB code: 7tzz:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 7tzz

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Magnesium binding site 1 out of 5 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T 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 P197T Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:61.4
occ:1.00
 O A:HIS567 2.1 60.6 1.0
O A:HOH907 2.2 64.7 1.0
OD1 A:ASP538 2.4 59.9 1.0
OD1 A:ASN565 2.4 61.1 1.0
OAT A:AUJ704 2.5 63.0 0.8
OAK A:AUJ704 2.6 57.3 0.8
PBE A:AUJ704 3.1 68.9 0.8
OAI A:AUJ704 3.1 73.0 0.8
C A:HIS567 3.4 57.5 1.0
CG A:ASN565 3.4 59.6 1.0
PBD A:AUJ704 3.5 61.6 0.8
CG A:ASP538 3.5 61.2 1.0
N A:ASP538 3.7 59.0 1.0
ND2 A:ASN565 3.8 63.6 1.0
N A:GLY569 4.0 56.3 1.0
N A:HIS567 4.0 59.1 1.0
OAG A:AUJ704 4.1 63.8 0.8
N A:GLY539 4.1 52.8 1.0
OD2 A:ASP538 4.1 61.8 1.0
OAS A:AUJ704 4.2 66.8 0.8
OAF A:AUJ704 4.2 65.0 0.8
CA A:HIS567 4.3 56.6 1.0
N A:LEU568 4.3 58.1 1.0
CA A:LEU568 4.4 58.1 1.0
C A:GLY537 4.5 58.5 1.0
CA A:GLY537 4.5 54.0 1.0
N A:ASN565 4.5 59.2 1.0
CA A:ASP538 4.5 57.6 1.0
CD1 A:LEU588 4.6 52.8 1.0
CB A:ASP538 4.6 55.4 1.0
O A:LEU563 4.7 61.8 1.0
CB A:ASN565 4.7 56.5 1.0
C A:LEU568 4.8 60.6 1.0
CA A:GLY569 4.8 59.9 1.0
N A:GLN566 4.8 54.6 1.0
OAJ A:AUJ704 4.8 55.9 0.8
C A:ASP538 4.8 55.5 1.0
C A:ASN565 4.9 59.5 1.0
CA A:ASN565 5.0 53.8 1.0

Magnesium binding site 2 out of 5 in 7tzz

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Magnesium binding site 2 out of 5 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T 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 2 of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg706

b:55.4
occ:0.71
 O A:MET543 2.6 53.9 1.0
OE1 A:GLN546 2.8 49.5 1.0
O A:HOH917 3.0 59.9 1.0
CD A:GLN546 3.7 51.3 1.0
C A:MET543 3.8 53.0 1.0
OD1 A:ASN544 4.0 53.0 1.0
NE2 A:GLN546 4.2 49.6 1.0
CA A:ASN544 4.3 54.7 1.0
CD2 A:HIS143 4.4 60.2 1.0
N A:ASN544 4.5 54.4 1.0
CA A:MET543 4.8 55.0 1.0
CG A:GLN546 4.8 47.7 1.0
CG A:ASN544 4.9 55.9 1.0
NE2 A:HIS143 5.0 58.7 1.0

Magnesium binding site 3 out of 5 in 7tzz

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Magnesium binding site 3 out of 5 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T 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 3 of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg707

b:121.2
occ:0.68
 NE2 A:GLN291 2.7 109.5 1.0
CD A:GLN291 3.6 111.2 1.0
CG A:GLN291 3.9 96.9 1.0
OE1 A:GLN291 4.7 95.9 1.0
CD2 A:LEU295 4.9 75.3 1.0
CG2 A:VAL409 4.9 89.1 1.0
CG A:LEU295 5.0 77.1 1.0

Magnesium binding site 4 out of 5 in 7tzz

Go back to Magnesium Binding Sites List in 7tzz
Magnesium binding site 4 out of 5 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T 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 4 of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg708

b:68.0
occ:1.00
 NE2 A:GLN207 2.5 53.0 1.0
OG1 A:THR167 2.6 54.5 1.0
OG A:SER168 2.9 49.8 1.0
N A:ALA122 3.0 52.1 1.0
CB A:ALA122 3.4 47.1 1.0
CD A:GLN207 3.6 59.1 1.0
N A:SER168 3.7 50.6 1.0
N A:GLY121 3.7 53.1 1.0
CB A:THR167 3.8 49.7 1.0
CG2 A:THR167 3.8 48.9 1.0
CA A:ALA122 3.8 55.2 1.0
CB A:GLN207 4.0 52.7 1.0
C A:GLY121 4.0 57.4 1.0
CB A:SER168 4.0 50.5 1.0
CA A:GLY121 4.0 52.4 1.0
CA A:SER168 4.3 49.9 1.0
O A:SER168 4.3 51.9 1.0
CG A:GLN207 4.3 54.5 1.0
C A:GLY120 4.3 55.2 1.0
OE1 A:GLN207 4.4 62.7 1.0
C A:SER168 4.5 55.1 1.0
C A:THR167 4.6 51.2 1.0
CA A:THR167 4.7 49.4 1.0
CA A:GLY120 4.7 50.2 1.0
C A:ALA122 4.9 55.0 1.0
O A:GLY120 5.0 52.6 1.0
O A:GLN207 5.0 53.1 1.0

Magnesium binding site 5 out of 5 in 7tzz

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Magnesium binding site 5 out of 5 in the Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T 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 5 of Crystal Structure of Arabidopsis Thaliana Acetohydroxyacid Synthase P197T Mutant in Complex with Bispyribac-Sodium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg711

b:87.0
occ:0.50
 NZ A:LYS618 2.4 70.9 1.0
OG1 A:THR457 3.4 62.9 1.0
CD1 A:TYR466 3.6 70.8 1.0
CE A:LYS618 3.6 78.6 1.0
CE1 A:TYR466 3.7 77.0 1.0
CE2 A:PHE455 3.9 65.2 1.0
CZ A:PHE455 3.9 61.9 1.0
O A:HOH880 4.1 63.7 0.5
CG A:TYR466 4.4 65.2 1.0
CZ A:TYR466 4.6 78.2 1.0
CB A:THR457 4.7 65.0 1.0
CD A:LYS618 4.9 73.0 1.0
CB A:TYR466 5.0 65.8 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 09:36:36 2024

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