Bromine in PDB 7v45: Crystal Structure of An Enzyme From Rhodococcus Coprophilus in Complex with S3

The structure of Crystal Structure of An Enzyme From Rhodococcus Coprophilus in Complex with S3, PDB code: 7v45 was solved by L.L.Zhang, J.W.Huang, W.D.Liu, C.C.Chen, R.T.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.22 / 1.45
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.036, 111.036, 80.708, 90, 90, 120
R / Rfree (%)	14.2 / 16.1

The structure of Crystal Structure of An Enzyme From Rhodococcus Coprophilus in Complex with S3 also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Bromine atom in the Crystal Structure of An Enzyme From Rhodococcus Coprophilus in Complex with S3 (pdb code 7v45). 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 An Enzyme From Rhodococcus Coprophilus in Complex with S3, PDB code: 7v45:

Bromine binding site 1 out of 1 in the Crystal Structure of An Enzyme From Rhodococcus Coprophilus in Complex with S3


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 An Enzyme From Rhodococcus Coprophilus in Complex with S3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:15.5 occ:1.00 BR A:C5O501 0.0 15.5 1.0 CAH A:C5O501 1.9 8.5 1.0 CAF A:C5O501 2.8 9.5 1.0 CAG A:C5O501 2.8 10.6 1.0 CD1 A:LEU110 4.0 8.0 1.0 CB A:ALA275 4.0 9.8 1.0 CAC A:C5O501 4.1 9.6 1.0 CAD A:C5O501 4.1 9.2 1.0 CA A:ALA275 4.1 8.9 1.0 CB A:ALA112 4.2 7.6 1.0 CZ A:PHE198 4.3 7.6 1.0 CG A:PRO114 4.4 5.6 1.0 N A:ALA275 4.5 8.1 1.0 CE2 A:PHE198 4.5 7.2 1.0 CD A:PRO114 4.6 5.3 1.0 CG1 A:VAL274 4.7 8.0 1.0 CAB A:C5O501 4.7 8.7 1.0 CE1 A:TYR115 4.8 6.1 1.0

C.C.Chen, M.Dai, L.Zhang, J.Zhao, W.Zeng, M.Shi, J.W.Huang, W.Liu, R.T.Guo, A.Li. Molecular Basis For A Toluene Monooxygenase to Govern Substrate Selectivity Acs Catalysis V. 12 2831 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C05845