Bromine in PDB 7z97: Crystal Structure of the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole

The structure of Crystal Structure of the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole, PDB code: 7z97 was solved by J.Kratky, R.Weisse, N.Strater, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.02 / 1.46
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.863, 95.863, 111.522, 90, 90, 120
R / Rfree (%)	17 / 20.8

The binding sites of Bromine atom in the Crystal Structure of the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole (pdb code 7z97). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole, PDB code: 7z97:

Bromine binding site 1 out of 1 in the Crystal Structure of the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole


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 the F191M Variant of Variovorax Paradoxus Indole Monooxygenase (VPINDA1) in Complex with 6-Bromoindole within 5.0Å range: probe atom residue distance (Å) B Occ A:Br503 b:44.8 occ:0.61 BR A:FK1503 0.0 44.8 0.6 C A:FK1503 1.9 37.1 0.6 C7 A:FK1503 2.8 37.6 0.6 C1 A:FK1503 2.8 36.8 0.6 HG11 A:VAL189 2.8 47.7 1.0 HZ A:PHE50 2.9 44.7 1.0 HD13 A:ILE75 3.0 51.0 1.0 HG21 A:VAL189 3.2 49.1 1.0 CE2 A:PHE385 3.4 41.7 1.0 CD2 A:PHE385 3.4 41.1 1.0 HE2 A:PHE385 3.4 50.7 1.0 HD2 A:PHE385 3.4 50.0 1.0 HD11 A:ILE75 3.4 51.0 1.0 CD1 A:ILE75 3.6 42.0 1.0 HB A:VAL189 3.7 47.6 1.0 CG1 A:VAL189 3.7 39.2 1.0 CZ A:PHE50 3.8 36.8 1.0 HG12 A:ILE75 3.9 52.1 1.0 CB A:VAL189 4.0 39.1 1.0 CZ A:PHE385 4.0 40.6 1.0 CG2 A:VAL189 4.0 40.4 1.0 CG A:PHE385 4.0 37.9 1.0 HG12 A:VAL189 4.1 47.7 1.0 C6 A:FK1503 4.1 35.6 0.6 C2 A:FK1503 4.1 34.4 0.6 HE1 A:PHE50 4.3 43.7 1.0 HG23 A:ILE75 4.3 50.0 1.0 CG1 A:ILE75 4.4 42.9 1.0 HD12 A:ILE75 4.4 51.0 1.0 SD A:MET191 4.4 60.6 1.0 HG13 A:VAL189 4.4 47.7 1.0 HZ A:PHE385 4.4 49.3 1.0 HB3 A:PHE385 4.5 43.9 1.0 HG21 A:ILE75 4.5 50.0 1.0 CE1 A:PHE50 4.5 35.9 1.0 HA3 A:GLY304 4.5 46.0 1.0 HG2 A:MET191 4.6 66.3 1.0 CD1 A:PHE385 4.6 39.8 1.0 HE2 A:PHE50 4.6 44.3 1.0 CE1 A:PHE385 4.6 41.0 1.0 HG23 A:VAL189 4.6 49.1 1.0 HG22 A:VAL189 4.6 49.1 1.0 O A:THR303 4.6 37.2 1.0 C3 A:FK1503 4.7 33.8 0.6 CE2 A:PHE50 4.7 36.4 1.0 HG A:CYS48 4.7 53.2 1.0 CB A:PHE385 4.8 36.0 1.0 CG2 A:ILE75 4.8 41.1 1.0 HB2 A:PHE385 4.9 43.9 1.0

J.Kratky, D.Eggerichs, T.Heine, S.Hofmann, P.Sowa, R.H.Weisse, D.Tischler, N.Strater. Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VPINDA1: New Avenues For Biocatalytic Epoxidations and Sulfoxidations. Angew.Chem.Int.Ed.Engl. 00657 2023.
ISSN: ESSN 1521-3773
PubMed: 36762980
DOI: 10.1002/ANIE.202300657