Mercury 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:

Bromine

(Br)

1 atom

The binding sites of Mercury 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 Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S, PDB code: 5c0t:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg 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:Hg301 b:36.6 occ:0.82 SG A:CYS159 2.4 34.5 1.0 SG A:CYS96 2.5 22.4 1.0 O A:HOH523 2.6 33.4 1.0 OG A:SER99 3.1 28.5 1.0 CD2 A:PHE158 3.6 29.9 1.0 CE2 A:PHE158 3.7 25.6 1.0 CB A:CYS159 3.7 33.0 1.0 CB A:CYS96 3.8 20.9 1.0 CA A:CYS159 4.1 29.9 1.0 CB A:SER99 4.5 24.0 1.0 N A:CYS159 4.5 29.9 1.0 CB A:TRP95 4.7 25.9 1.0 N A:CYS96 4.8 21.3 1.0 N A:SER99 4.8 16.5 1.0 CA A:CYS96 4.9 20.8 1.0 CG A:PHE158 4.9 29.7 1.0 CG2 A:VAL154 5.0 59.6 1.0 CA A:SER99 5.0 20.8 1.0

Mercury binding site 2 out of 2 in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg301 b:36.0 occ:0.77 SG B:CYS159 2.4 35.7 1.0 SG B:CYS96 2.5 25.1 1.0 O B:HOH498 2.7 31.8 1.0 OG B:SER99 3.1 27.1 1.0 CB B:CYS159 3.6 27.7 1.0 CD2 B:PHE158 3.8 25.9 1.0 CB B:CYS96 3.8 18.7 1.0 CA B:CYS159 4.0 26.5 1.0 CE2 B:PHE158 4.0 24.5 1.0 CG2 B:VAL154 4.3 48.6 1.0 N B:CYS159 4.3 27.6 1.0 CB B:SER99 4.5 20.0 1.0 N B:SER99 4.7 20.4 1.0 N B:CYS96 4.7 22.0 1.0 CB B:TRP95 4.8 23.3 1.0 CA B:CYS96 4.9 22.4 1.0 CA B:SER99 5.0 22.6 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