Bromine in PDB 3ns2: High-Resolution Structure of Pyrabactin-Bound PYL2

The structure of High-Resolution Structure of Pyrabactin-Bound PYL2, PDB code: 3ns2 was solved by Q.Hao, P.Yin, C.Yan, X.Yuan, J.Wang, N.Yan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.38 / 1.63
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	62.520, 104.600, 184.300, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 21.8

The binding sites of Bromine atom in the High-Resolution Structure of Pyrabactin-Bound PYL2 (pdb code 3ns2). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the High-Resolution Structure of Pyrabactin-Bound PYL2, PDB code: 3ns2:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the High-Resolution Structure of Pyrabactin-Bound PYL2


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of High-Resolution Structure of Pyrabactin-Bound PYL2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br191 b:51.4 occ:0.62 BR A:PYV191 0.0 51.4 0.6 C1 A:PYV191 1.9 46.0 0.6 C6 A:PYV191 2.8 41.3 0.6 C2 A:PYV191 2.9 54.0 0.6 C10 A:PYV191 3.2 57.5 0.6 CE2 A:PHE165 3.3 35.6 1.0 CG2 A:VAL169 3.7 24.9 1.0 CB A:VAL169 3.7 21.5 1.0 CZ A:PHE165 3.8 30.5 1.0 CD2 A:PHE165 3.9 31.0 1.0 CG1 A:VAL169 4.0 26.4 1.0 CD1 A:LEU121 4.0 43.3 1.0 CG2 A:VAL166 4.0 25.1 1.0 C5 A:PYV191 4.2 40.2 0.6 CA A:VAL166 4.2 19.8 1.0 C3 A:PYV191 4.3 49.8 0.6 C15 A:PYV191 4.3 45.8 0.6 C14 A:PYV191 4.3 58.5 0.6 CG1 A:VAL166 4.4 20.5 1.0 CB A:VAL166 4.5 21.6 1.0 C9 A:PYV191 4.6 55.2 0.6 CE1 A:PHE165 4.7 31.2 1.0 C4 A:PYV191 4.7 48.3 0.6 O A:PHE165 4.8 23.0 1.0 CG A:PHE165 4.8 28.0 1.0 N A:VAL166 4.9 21.0 1.0 C16 A:PYV191 5.0 40.9 0.6

Bromine binding site 2 out of 3 in the High-Resolution Structure of Pyrabactin-Bound PYL2


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of High-Resolution Structure of Pyrabactin-Bound PYL2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br191 b:48.9 occ:0.68 BR B:PYV191 0.0 48.9 0.7 C1 B:PYV191 1.9 41.1 0.7 C6 B:PYV191 2.9 36.2 0.7 C2 B:PYV191 2.9 49.2 0.7 C10 B:PYV191 3.1 41.8 0.7 CE2 B:PHE165 3.2 36.2 1.0 CD2 B:PHE165 3.8 33.6 1.0 CZ B:PHE165 3.8 34.2 1.0 CG2 B:VAL169 3.8 26.5 1.0 CB B:VAL169 3.9 20.7 1.0 CA B:VAL166 4.0 19.6 1.0 CG2 B:VAL166 4.1 25.9 1.0 CG1 B:VAL169 4.1 23.9 1.0 C5 B:PYV191 4.2 38.6 0.7 C3 B:PYV191 4.3 51.5 0.7 CB B:VAL166 4.4 20.5 1.0 CG1 B:VAL166 4.4 22.7 1.0 C15 B:PYV191 4.5 49.3 0.7 C9 B:PYV191 4.5 41.7 0.7 O B:PHE165 4.7 22.8 1.0 N B:VAL166 4.7 22.3 1.0 CG B:PHE165 4.7 29.3 1.0 CE1 B:PHE165 4.7 33.4 1.0 C4 B:PYV191 4.8 47.3 0.7 C14 B:PYV191 4.8 52.1 0.7 C B:PHE165 4.9 28.8 1.0 O B:VAL166 5.0 21.5 1.0

Bromine binding site 3 out of 3 in the High-Resolution Structure of Pyrabactin-Bound PYL2


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of High-Resolution Structure of Pyrabactin-Bound PYL2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br191 b:43.7 occ:0.66 BR C:PYV191 0.0 43.7 0.7 C1 C:PYV191 1.9 37.4 0.7 C6 C:PYV191 2.9 31.6 0.7 C2 C:PYV191 2.9 44.1 0.7 C10 C:PYV191 3.1 48.3 0.7 CE2 C:PHE165 3.3 35.5 1.0 CG2 C:VAL169 3.7 29.5 1.0 CB C:VAL169 3.7 24.9 1.0 CD2 C:PHE165 3.9 35.9 1.0 CZ C:PHE165 3.9 30.9 1.0 CG1 C:VAL169 3.9 28.4 1.0 CG2 C:VAL166 4.1 26.3 1.0 CA C:VAL166 4.1 22.4 1.0 CD2 C:LEU121 4.1 42.9 1.0 C5 C:PYV191 4.2 39.5 0.7 C3 C:PYV191 4.3 43.2 0.7 CG1 C:VAL166 4.3 28.6 1.0 CB C:VAL166 4.4 23.8 1.0 C15 C:PYV191 4.4 40.9 0.7 C9 C:PYV191 4.5 48.2 0.7 O C:PHE165 4.6 25.8 1.0 N C:VAL166 4.7 24.3 1.0 CG C:PHE165 4.8 29.9 1.0 C4 C:PYV191 4.8 43.5 0.7 CE1 C:PHE165 4.8 32.2 1.0 C C:PHE165 4.9 29.9 1.0 C14 C:PYV191 4.9 44.7 0.7 O C:VAL166 4.9 24.4 1.0 C16 C:PYV191 5.0 41.4 0.7

X.Yuan, P.Yin, Q.Hao, C.Yan, J.Wang, N.Yan. Single Amino Acid Alteration Between Valine and Isoleucine Determines the Distinct Pyrabactin Selectivity By PYL1 and PYL2 J.Biol.Chem. V. 285 28953 2010.
ISSN: ISSN 0021-9258
PubMed: 20630864
DOI: 10.1074/JBC.M110.160192