Bromine in PDB 1xu3: Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol

All present enzymatic activity of Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol:
1.14.13.25;

The structure of Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol, PDB code: 1xu3 was solved by M.H.Sazinsky, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.83 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.489, 171.856, 221.424, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.5

The structure of Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Bromine atom in the Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol (pdb code 1xu3). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol, PDB code: 1xu3:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1292 b:50.0 occ:1.00 BR4 A:BML1292 0.0 50.0 1.0 C4 A:BML1292 1.9 50.0 1.0 C3 A:BML1292 2.8 50.0 1.0 C5 A:BML1292 2.9 50.0 1.0 CE A:MET288 3.3 35.2 1.0 CD1 A:LEU180 3.6 22.7 1.0 CE1 A:PHE359 3.9 22.4 1.0 CD2 A:LEU289 3.9 28.5 1.0 CZ A:PHE359 4.1 22.6 1.0 C6 A:BML1292 4.1 50.0 1.0 C2 A:BML1292 4.2 50.0 1.0 SD A:MET288 4.3 37.6 1.0 CD2 A:LEU361 4.4 21.7 1.0 CB A:ALA350 4.6 30.6 1.0 CD1 A:PHE359 4.7 21.1 1.0 CG A:MET288 4.7 35.0 1.0 C1 A:BML1292 4.7 50.0 1.0 CG2 A:VAL105 4.9 27.2 1.0 CG A:LEU289 4.9 32.5 1.0

Bromine binding site 2 out of 2 in the Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Soluble Methane Monooxygenase Hydroxylase-Soaked with Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1293 b:46.0 occ:1.00 BR4 B:BML1293 0.0 46.0 1.0 C4 B:BML1293 1.8 46.0 1.0 C3 B:BML1293 2.8 46.0 1.0 C5 B:BML1293 2.9 46.0 1.0 CD1 B:LEU180 3.4 25.0 1.0 CE B:MET288 3.6 26.7 1.0 CE1 B:PHE359 3.8 23.6 1.0 CZ B:PHE359 3.8 24.2 1.0 CD2 B:LEU289 4.1 30.0 1.0 C6 B:BML1293 4.1 46.0 1.0 C2 B:BML1293 4.2 46.0 1.0 CD2 B:LEU361 4.4 23.7 1.0 SD B:MET288 4.5 29.6 1.0 CB B:ALA350 4.6 24.2 1.0 CD1 B:PHE359 4.7 25.4 1.0 CE2 B:PHE359 4.7 25.7 1.0 C1 B:BML1293 4.7 46.0 1.0 CG B:MET288 4.8 28.9 1.0 CG B:LEU180 5.0 27.4 1.0

M.H.Sazinsky, S.J.Lippard. Product Bound Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath): Protein Motion in the Alpha-Subunit J.Am.Chem.Soc. V. 127 5814 2005.
ISSN: ISSN 0002-7863
PubMed: 15839679
DOI: 10.1021/JA044099B