Bromine in PDB 5c0t: Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S

All present enzymatic activity of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S:
4.99.1.2;

The structure of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S, PDB code: 5c0t was solved by H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, J.Sygusch, D.E.Wilcox, J.G.Omichinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.20 / 1.96
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.061, 89.113, 51.824, 90.00, 100.79, 90.00
R / Rfree (%)	16.4 / 20.8

The structure of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S also contains other interesting chemical elements:

Mercury

(Hg)

2 atoms

The binding sites of Bromine atom in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S (pdb code 5c0t). 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 Mercury-Bound Form of Merb Mutant D99S, PDB code: 5c0t:

Bromine binding site 1 out of 1 in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S


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 Mercury-Bound Form of Merb Mutant D99S within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:21.2 occ:0.48 O A:HOH518 3.3 31.2 1.0 O A:HOH539 3.3 40.6 1.0 CD A:PRO5 3.6 25.8 1.0 CD A:LYS2 3.7 52.0 1.0 CG A:PRO5 3.9 27.0 1.0 CB A:LYS2 3.9 40.9 1.0 CB A:ALA4 4.1 27.9 1.0 CG A:LYS2 4.4 46.7 1.0 N A:PRO5 4.7 25.6 1.0 CE A:LYS2 4.8 56.0 1.0 N A:ALA4 4.9 30.3 1.0 CA A:ALA4 5.0 27.6 1.0

H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, J.Sygusch, D.E.Wilcox, J.G.Omichinski. Structural and Biochemical Characterization of A Copper-Binding Mutant of the Organomercurial Lyase Merb: Insight Into the Key Role of the Active Site Aspartic Acid in Hg-Carbon Bond Cleavage and Metal Binding Specificity. Biochemistry V. 55 1070 2016.
ISSN: ISSN 0006-2960
PubMed: 26820485
DOI: 10.1021/ACS.BIOCHEM.5B01298