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Magnesium in PDB 5jo2: Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1

Enzymatic activity of Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1

All present enzymatic activity of Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1, PDB code: 5jo2 was solved by J.K.Weng, J.P.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.25 / 2.42
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 45.330, 75.310, 169.200, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1 (pdb code 5jo2). 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 Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1, PDB code: 5jo2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5jo2

Go back to Magnesium Binding Sites List in 5jo2
Magnesium binding site 1 out of 2 in the Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1


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 Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:31.6
occ:1.00
OD2 B:ASP492 2.0 67.5 1.0
O B:HOH703 2.1 32.8 1.0
O B:HOH706 2.1 39.6 1.0
OD2 B:ASP243 2.1 53.2 1.0
OD1 B:ASP432 2.6 47.8 1.0
MG B:MG602 2.8 44.3 1.0
CG B:ASP492 2.8 63.9 1.0
CG B:ASP243 2.9 48.3 1.0
OD1 B:ASP243 3.0 43.9 1.0
OD1 B:ASP492 3.1 68.6 1.0
CG B:ASP432 3.7 49.0 1.0
O B:HOH707 4.1 42.4 1.0
OD2 B:ASP432 4.1 56.9 1.0
CB B:ASP492 4.2 47.1 1.0
CB B:ASP243 4.4 43.7 1.0
OD1 B:ASP204 4.4 59.3 1.0
O B:ASN493 4.4 47.5 1.0
N B:GLY433 4.7 50.3 1.0
N B:ASP432 4.8 40.8 1.0
NH1 B:ARG199 4.8 68.0 1.0
OD2 B:ASP204 4.8 47.5 1.0
CB B:SER431 4.9 37.8 1.0
CB B:ASP432 4.9 42.7 1.0
C B:ASP432 5.0 49.6 1.0
N B:ASN493 5.0 46.6 1.0

Magnesium binding site 2 out of 2 in 5jo2

Go back to Magnesium Binding Sites List in 5jo2
Magnesium binding site 2 out of 2 in the Crystal Structure of Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1


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 Abscisic Acid-Bound Abscisic Acid Receptor PYL3 in Complex with Type 2C Protein Phosphatase HAB1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:44.3
occ:1.00
O B:HOH707 2.1 42.4 1.0
OD1 B:ASP243 2.3 43.9 1.0
O B:GLY244 2.7 46.0 1.0
MG B:MG601 2.8 31.6 1.0
CG B:ASP243 3.2 48.3 1.0
O B:HOH703 3.5 32.8 1.0
OD2 B:ASP243 3.6 53.2 1.0
OD1 B:ASP492 3.8 68.6 1.0
C B:GLY244 3.9 41.2 1.0
O B:HOH706 4.0 39.6 1.0
OD1 B:ASP204 4.1 59.3 1.0
OD2 B:ASP492 4.1 67.5 1.0
OE2 B:GLU203 4.2 81.4 1.0
NH1 B:ARG199 4.3 68.0 1.0
CG B:ASP492 4.4 63.9 1.0
OD1 B:ASN493 4.4 48.1 1.0
CB B:ASP243 4.6 43.7 1.0
C B:ASP243 4.6 37.9 1.0
N B:GLY244 4.6 36.7 1.0
CB B:HIS245 4.7 41.7 1.0
CA B:HIS245 4.7 43.0 1.0
N B:HIS245 4.8 40.5 1.0
O B:ASP243 4.9 36.5 1.0
CA B:GLY244 4.9 39.3 1.0
CA B:ASP243 4.9 39.2 1.0

Reference:

J.K.Weng, M.Ye, B.Li, J.P.Noel. Co-Evolution of Hormone Metabolism and Signaling Networks Expands Plant Adaptive Plasticity. Cell V. 166 881 2016.
ISSN: ISSN 1097-4172
PubMed: 27518563
DOI: 10.1016/J.CELL.2016.06.027
Page generated: Sun Sep 29 17:53:05 2024

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