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Magnesium in PDB 4la7: X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex

Enzymatic activity of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex

All present enzymatic activity of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex:
3.1.3.16;

Protein crystallography data

The structure of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex, PDB code: 4la7 was solved by F.C.Peterson, B.F.Volkman, S.R.Cutler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.27 / 1.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.637, 66.754, 146.021, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 22.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex (pdb code 4la7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex, PDB code: 4la7:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4la7

Go back to Magnesium Binding Sites List in 4la7
Magnesium binding site 1 out of 4 in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:20.0
occ:1.00
OD2 B:ASP243 1.9 18.5 1.0
O B:HOH873 2.0 21.3 1.0
OD2 B:ASP432 2.0 24.1 1.0
OD2 B:ASP492 2.1 28.2 1.0
O B:HOH869 2.2 19.6 1.0
O B:HOH868 2.2 16.9 1.0
CG B:ASP243 2.9 17.7 1.0
CG B:ASP432 2.9 20.6 1.0
OD1 B:ASP432 3.1 31.2 1.0
OD1 B:ASP243 3.2 22.2 1.0
CG B:ASP492 3.2 24.5 1.0
O B:HOH872 3.5 23.7 1.0
OD1 B:ASP492 3.5 24.9 1.0
MG B:MG602 3.7 24.6 1.0
MG B:MG604 4.0 28.4 1.0
O B:HOH780 4.0 24.9 1.0
O B:HOH784 4.2 37.7 1.0
O B:HOH744 4.2 43.3 1.0
CB B:ASP243 4.2 11.8 1.0
O B:HOH870 4.3 16.9 1.0
CB B:ASP432 4.3 25.4 1.0
N B:GLY433 4.3 19.1 1.0
OD1 B:ASP204 4.4 26.6 1.0
N B:ASP432 4.4 22.3 1.0
CB B:ASP492 4.5 21.8 1.0
O B:ASN493 4.6 23.6 1.0
CA B:ASP432 4.7 20.3 1.0
CB B:SER431 4.7 15.2 1.0
C B:ASP432 4.8 22.5 1.0
O B:HOH892 4.9 36.2 1.0
O B:HOH707 5.0 22.6 1.0
OG B:SER431 5.0 20.1 1.0

Magnesium binding site 2 out of 4 in 4la7

Go back to Magnesium Binding Sites List in 4la7
Magnesium binding site 2 out of 4 in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:24.6
occ:1.00
O B:HOH872 1.9 23.7 1.0
O B:HOH871 1.9 15.4 1.0
O B:HOH873 2.1 21.3 1.0
O B:HOH870 2.1 16.9 1.0
O B:GLY244 2.2 22.9 1.0
OD1 B:ASP243 2.3 22.2 1.0
CG B:ASP243 3.4 17.7 1.0
C B:GLY244 3.4 23.3 1.0
MG B:MG601 3.7 20.0 1.0
O B:HOH744 3.7 43.3 1.0
OD2 B:ASP243 3.8 18.5 1.0
O B:HOH707 3.9 22.6 1.0
OE1 B:GLU203 4.0 22.2 1.0
N B:GLY244 4.0 15.1 1.0
OD1 B:ASP204 4.1 26.6 1.0
O B:HOH869 4.1 19.6 1.0
CB B:GLU203 4.2 19.1 1.0
C B:ASP243 4.2 18.9 1.0
N B:HIS245 4.3 24.7 1.0
CA B:GLY244 4.4 18.6 1.0
CA B:HIS245 4.4 21.2 1.0
OD1 B:ASP492 4.4 24.9 1.0
O B:HOH868 4.4 16.9 1.0
OD1 B:ASN493 4.5 21.1 1.0
O B:HOH747 4.5 42.3 1.0
CB B:HIS245 4.6 19.5 1.0
O B:ASP243 4.6 18.0 1.0
CB B:ASP243 4.6 11.8 1.0
CA B:ASP243 4.7 17.7 1.0
NH2 B:ARG199 4.7 39.1 1.0
CG B:GLU203 4.8 26.9 1.0
OD2 B:ASP492 4.8 28.2 1.0
CD B:GLU203 4.9 29.1 1.0

Magnesium binding site 3 out of 4 in 4la7

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Magnesium binding site 3 out of 4 in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg604

b:28.4
occ:1.00
OD1 B:ASP346 2.5 29.7 1.0
OD2 B:ASP243 2.8 18.5 1.0
N B:ASP432 2.8 22.3 1.0
CG B:ASP432 3.1 20.6 1.0
OG B:SER347 3.2 30.6 1.0
OD2 B:ASP432 3.2 24.1 1.0
CB B:ASP432 3.3 25.4 1.0
CB B:ASP243 3.4 11.8 1.0
CG B:ASP243 3.5 17.7 1.0
O B:HOH780 3.6 24.9 1.0
OD1 B:ASP432 3.6 31.2 1.0
CA B:ASP432 3.6 20.3 1.0
CG B:ASP346 3.6 23.9 1.0
N B:SER347 3.7 23.6 1.0
C B:SER431 3.7 21.2 1.0
CA B:SER347 3.7 24.1 1.0
CA B:SER431 3.7 18.0 1.0
O B:ASP346 3.8 25.1 1.0
C B:ASP346 3.8 22.5 1.0
CB B:SER431 3.9 15.2 1.0
MG B:MG601 4.0 20.0 1.0
CB B:SER347 4.1 28.7 1.0
CG2 B:THR328 4.2 18.0 1.0
OD2 B:ASP346 4.2 38.8 1.0
OG1 B:THR328 4.3 21.4 1.0
O B:HOH869 4.6 19.6 1.0
OD1 B:ASP243 4.6 22.2 1.0
CA B:ASP346 4.7 24.2 1.0
CB B:ASP346 4.7 25.4 1.0
CB B:THR328 4.8 18.8 1.0
O B:HOH868 4.8 16.9 1.0
C B:ASP432 4.8 22.5 1.0
O B:SER431 4.9 19.6 1.0
CA B:ASP243 4.9 17.7 1.0

Magnesium binding site 4 out of 4 in 4la7

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Magnesium binding site 4 out of 4 in the X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of X-Ray Crystal Structure of the PYL2-Quinabactin-HAB1 Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg605

b:27.1
occ:1.00
O B:HOH821 3.2 30.9 1.0
N B:HIS248 3.2 23.9 1.0
N B:LYS249 3.3 22.0 1.0
CB B:LYS249 3.5 21.9 1.0
CA B:GLY247 3.6 23.4 1.0
CG B:LYS249 3.6 31.1 1.0
CD B:LYS249 3.6 33.1 1.0
C B:GLY247 3.7 23.5 1.0
CA B:LYS249 4.0 28.1 1.0
CG2 B:VAL325 4.1 24.5 1.0
ND1 B:HIS248 4.2 35.0 1.0
CA B:HIS248 4.2 27.3 1.0
C B:HIS248 4.3 30.9 1.0
CG1 B:VAL325 4.3 17.3 1.0
CE1 B:HIS248 4.4 31.9 1.0
CG B:HIS248 4.5 29.2 1.0
CE B:LYS249 4.6 42.3 1.0
CB B:VAL325 4.7 22.7 1.0
NE2 B:HIS248 4.8 32.0 1.0
O B:GLY247 4.8 22.5 1.0
O B:HOH845 4.8 55.9 1.0
CD2 B:HIS248 4.8 25.6 1.0
N B:GLY247 4.8 22.3 1.0
CB B:ALA321 4.8 27.3 1.0
NZ B:LYS249 4.8 44.3 1.0
O B:GLY246 4.9 27.9 1.0
CB B:HIS248 4.9 21.4 1.0

Reference:

M.Okamoto, F.C.Peterson, A.Defries, S.Y.Park, A.Endo, E.Nambara, B.F.Volkman, S.R.Cutler. Activation of Dimeric Aba Receptors Elicits Guard Cell Closure, Aba-Regulated Gene Expression, and Drought Tolerance. Proc.Natl.Acad.Sci.Usa V. 110 12132 2013.
ISSN: ISSN 0027-8424
PubMed: 23818638
DOI: 10.1073/PNAS.1305919110
Page generated: Sat Aug 17 04:52:07 2024

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