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Bromine in PDB 3nmn: Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1

Enzymatic activity of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1

All present enzymatic activity of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1, PDB code: 3nmn was solved by X.E.Zhou, K.Melcher, L.-M.Ng, F.-F.Soon, Y.Xu, K.M.Suino-Powell, A.Kovach, J.Li, E.-L.Yong, H.E.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.62 / 2.15
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 59.978, 66.710, 72.598, 115.78, 95.43, 105.60
R / Rfree (%) 21 / 24.8

Other elements in 3nmn:

The structure of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1 also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1 (pdb code 3nmn). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1, PDB code: 3nmn:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in 3nmn

Go back to Bromine Binding Sites List in 3nmn
Bromine binding site 1 out of 2 in the Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br900

b:25.2
occ:1.00
BR A:PYV900 0.0 25.2 1.0
C1 A:PYV900 1.5 37.0 1.0
C6 A:PYV900 2.5 43.1 1.0
C2 A:PYV900 2.7 39.8 1.0
C10 A:PYV900 3.1 37.8 1.0
CZ A:PHE189 3.5 33.4 1.0
CD1 A:LEU114 3.7 51.5 1.0
C5 A:PYV900 3.9 43.5 1.0
CE2 A:PHE189 3.9 34.4 1.0
C3 A:PYV900 4.1 38.6 1.0
CD A:PRO115 4.2 44.9 1.0
CG1 A:VAL193 4.4 32.6 1.0
CB A:LEU114 4.5 48.5 1.0
C9 A:PYV900 4.5 36.3 1.0
C4 A:PYV900 4.5 41.9 1.0
CE1 A:PHE189 4.6 34.5 1.0
CB A:ALA116 4.6 43.8 1.0
CG A:LEU114 4.7 49.4 1.0
CG A:PRO115 4.8 46.6 1.0
N A:ALA116 4.9 44.2 1.0

Bromine binding site 2 out of 2 in 3nmn

Go back to Bromine Binding Sites List in 3nmn
Bromine binding site 2 out of 2 in the Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Pyrabactin-Bound Abscisic Acid Receptor PYL1 in Complex with Type 2C Protein Phosphatase ABI1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br900

b:31.3
occ:1.00
BR C:PYV900 0.0 31.3 1.0
C1 C:PYV900 1.5 41.0 1.0
C6 C:PYV900 2.5 45.0 1.0
C2 C:PYV900 2.7 43.0 1.0
C10 C:PYV900 3.0 44.2 1.0
CD1 C:LEU114 3.5 25.8 1.0
CZ C:PHE189 3.5 39.7 1.0
CE2 C:PHE189 3.8 39.7 1.0
C5 C:PYV900 3.9 43.4 1.0
C3 C:PYV900 4.1 43.0 1.0
CG2 C:VAL193 4.1 28.6 1.0
CD C:PRO115 4.3 23.7 1.0
CB C:LEU114 4.4 27.2 1.0
C9 C:PYV900 4.4 44.9 1.0
CG C:LEU114 4.5 26.9 1.0
C4 C:PYV900 4.6 42.4 1.0
CE1 C:PHE189 4.6 41.2 1.0
CG C:PRO115 4.8 24.7 1.0
CB C:ALA116 4.9 28.6 1.0

Reference:

K.Melcher, Y.Xu, L.M.Ng, X.E.Zhou, F.F.Soon, V.Chinnusamy, K.M.Suino-Powell, A.Kovach, F.S.Tham, S.R.Cutler, J.Li, E.L.Yong, J.K.Zhu, H.E.Xu. Identification and Mechanism of Aba Receptor Antagonism. Nat.Struct.Mol.Biol. V. 17 1102 2010.
ISSN: ISSN 1545-9993
PubMed: 20729862
DOI: 10.1038/NSMB.1887
Page generated: Mon Jul 7 05:42:29 2025

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