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Manganese in PDB 3qn1: Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain

Enzymatic activity of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain

All present enzymatic activity of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain, PDB code: 3qn1 was solved by K.Betz, F.Dupeux, J.Santiago, J.A.Marquez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.24 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.850, 65.860, 170.870, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain (pdb code 3qn1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain, PDB code: 3qn1:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 3qn1

Go back to Manganese Binding Sites List in 3qn1
Manganese binding site 1 out of 3 in the Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1

b:16.9
occ:1.00
 OD2 B:ASP243 2.1 15.2 1.0
OD1 B:ASP432 2.2 15.5 1.0
O B:HOH24 2.2 18.0 1.0
OD2 B:ASP492 2.2 17.5 1.0
O B:HOH16 2.3 15.9 1.0
O B:HOH669 2.3 18.6 1.0
CG B:ASP243 3.1 14.7 1.0
CG B:ASP492 3.2 17.7 1.0
CG B:ASP432 3.2 18.9 1.0
OD1 B:ASP243 3.3 14.4 1.0
OD1 B:ASP492 3.4 18.9 1.0
OD2 B:ASP432 3.5 20.5 1.0
MN B:MN2 3.9 27.3 1.0
O B:HOH125 4.0 21.2 1.0
O B:HOH513 4.2 16.8 1.0
O B:HOH25 4.2 19.4 1.0
N B:GLY433 4.2 13.4 1.0
O B:HOH11 4.3 16.5 1.0
CB B:ASP243 4.4 13.8 1.0
OD1 B:ASP204 4.4 15.4 1.0
O B:ASN493 4.5 15.3 1.0
N B:ASP432 4.5 14.1 1.0
CB B:ASP432 4.5 14.1 1.0
CB B:ASP492 4.5 17.6 1.0
C B:ASP432 4.7 14.8 1.0
CA B:ASP432 4.8 14.6 1.0
CB B:SER431 4.8 14.9 1.0
O B:HOH160 4.9 42.9 1.0

Manganese binding site 2 out of 3 in 3qn1

Go back to Manganese Binding Sites List in 3qn1
Manganese binding site 2 out of 3 in the Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn2

b:27.3
occ:1.00
 OD1 B:ASP243 2.2 14.4 1.0
O B:HOH669 2.2 18.6 1.0
O B:GLY244 2.2 15.6 1.0
O B:HOH11 2.3 16.5 1.0
O B:HOH33 2.3 15.5 1.0
O B:HOH125 2.4 21.2 1.0
CG B:ASP243 3.4 14.7 1.0
C B:GLY244 3.4 16.7 1.0
O B:HOH9 3.9 16.9 1.0
MN B:MN1 3.9 16.9 1.0
OD2 B:ASP243 3.9 15.2 1.0
O B:HOH160 4.0 42.9 1.0
N B:GLY244 4.0 15.5 1.0
C B:ASP243 4.1 15.2 1.0
O B:HOH24 4.3 18.0 1.0
CA B:GLY244 4.3 15.8 1.0
OE1 B:GLU203 4.3 18.1 1.0
N B:HIS245 4.3 16.5 1.0
CB B:GLU203 4.4 14.6 1.0
OD1 B:ASP204 4.4 15.4 1.0
O B:ASP243 4.4 14.3 1.0
O B:HOH16 4.5 15.9 1.0
CA B:HIS245 4.5 15.4 1.0
NH1 B:ARG199 4.6 26.7 1.0
ND2 B:ASN493 4.6 12.1 1.0
CB B:ASP243 4.6 13.8 1.0
OD1 B:ASP492 4.6 18.9 1.0
O B:HOH65 4.6 23.8 1.0
CA B:ASP243 4.7 14.2 1.0
CB B:HIS245 4.7 16.6 1.0
C B:GLU203 4.9 14.2 1.0
O B:GLU203 4.9 14.8 1.0

Manganese binding site 3 out of 3 in 3qn1

Go back to Manganese Binding Sites List in 3qn1
Manganese binding site 3 out of 3 in the Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the PYR1 Abscisic Acid Receptor in Complex with the HAB1 Type 2C Phosphatase Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn3

b:30.0
occ:1.00
 OD2 B:ASP432 2.2 20.5 1.0
O B:HOH89 2.3 25.7 1.0
O B:HOH575 2.3 29.6 1.0
O B:HOH647 2.3 29.9 1.0
OD2 B:ASP346 2.5 22.6 1.0
NZ B:LYS365 3.2 33.0 1.0
CG B:ASP432 3.3 18.9 1.0
CG B:ASP346 3.3 20.4 1.0
CB B:ASP432 3.7 14.1 1.0
OD1 B:ASP346 3.9 17.2 1.0
O B:HOH24 4.1 18.0 1.0
O B:HOH25 4.1 19.4 1.0
CE B:LYS365 4.2 30.2 1.0
CB B:ASP346 4.3 16.2 1.0
O B:HOH26 4.3 20.8 1.0
OD1 B:ASP432 4.3 15.5 1.0
OD1 B:ASP436 4.4 24.5 1.0
OD2 B:ASP436 4.4 28.5 1.0
O B:HOH624 4.8 38.8 1.0
CG B:ASP436 4.8 22.4 1.0

Reference:

F.Dupeux, R.Antoni, K.Betz, J.Santiago, M.Gonzalez-Guzman, L.Rodriguez, S.Rubio, S.Y.Park, S.R.Cutler, P.L.Rodriguez, J.A.Marquez. Modulation of Abscisic Acid Signaling in Vivo By An Engineered Receptor-Insensitive Protein Phosphatase Type 2C Allele. Plant Physiol. V. 156 106 2011.
ISSN: ISSN 0032-0889
PubMed: 21357183
DOI: 10.1104/PP.110.170894
Page generated: Tue Dec 15 04:14:29 2020

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