Copper in PDB 5c0u: Crystal Structure of the Copper-Bound Form of Merb Mutant D99S

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

The structure of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S, PDB code: 5c0u 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)	31.07 / 1.87
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.903, 88.958, 52.005, 90.00, 100.64, 90.00
R / Rfree (%)	14.7 / 19.2

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

Bromine

(Br)

1 atom

The binding sites of Copper atom in the Crystal Structure of the Copper-Bound Form of Merb Mutant D99S (pdb code 5c0u). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of the Copper-Bound Form of Merb Mutant D99S, PDB code: 5c0u:
Jump to Copper binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:29.9 occ:0.29 SG A:CYS159 2.2 26.4 1.0 SG A:CYS96 2.2 17.9 1.0 OG A:SER99 2.9 28.2 1.0 O A:HOH439 3.0 41.5 1.0 CB A:CYS96 3.2 14.9 1.0 CB A:CYS159 3.4 22.9 1.0 CA A:CYS159 3.9 21.0 1.0 CD2 A:PHE158 4.0 19.8 1.0 N A:CYS96 4.0 14.3 1.0 CE2 A:PHE158 4.1 19.0 1.0 CB A:TRP95 4.1 21.4 1.0 CA A:CYS96 4.2 13.3 1.0 CB A:SER99 4.2 13.7 1.0 C A:TRP95 4.3 13.2 1.0 N A:CYS159 4.5 22.6 1.0 N A:SER99 4.7 11.4 1.0 O A:TRP95 4.7 11.2 1.0 CA A:TRP95 4.8 11.0 1.0 C A:CYS96 4.9 11.2 1.0 CA A:SER99 4.9 16.9 1.0

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


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:27.2 occ:0.27 SG B:CYS96 2.2 19.8 1.0 SG B:CYS159 2.2 23.7 1.0 OG B:SER99 2.9 20.4 1.0 O B:HOH524 3.0 43.1 1.0 CB B:CYS159 3.2 18.8 1.0 CB B:CYS96 3.3 17.0 1.0 CA B:CYS159 3.7 15.2 1.0 CD2 B:PHE158 4.0 22.3 1.0 N B:CYS96 4.1 12.7 1.0 CB B:SER99 4.2 11.8 1.0 CB B:TRP95 4.2 11.8 1.0 CA B:CYS96 4.2 13.1 1.0 CE2 B:PHE158 4.3 22.0 1.0 N B:CYS159 4.3 20.0 1.0 C B:TRP95 4.4 11.2 1.0 N B:SER99 4.6 13.2 1.0 CG2 B:VAL154 4.6 53.2 1.0 O B:TRP95 4.8 13.4 1.0 CA B:SER99 4.8 16.2 1.0 CA B:TRP95 4.9 10.2 1.0 C B:CYS159 4.9 17.6 1.0 C B:CYS96 4.9 13.2 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