Mercury in PDB 2z9g: Complex Structure of Sars-Cov 3C-Like Protease with Pma

The structure of Complex Structure of Sars-Cov 3C-Like Protease with Pma, PDB code: 2z9g was solved by C.C.Lee, A.H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.86
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.280, 81.930, 53.450, 90.00, 104.99, 90.00
R / Rfree (%)	19.3 / 23.2

The binding sites of Mercury atom in the Complex Structure of Sars-Cov 3C-Like Protease with Pma (pdb code 2z9g). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Complex Structure of Sars-Cov 3C-Like Protease with Pma, PDB code: 2z9g:

Mercury binding site 1 out of 1 in the Complex Structure of Sars-Cov 3C-Like Protease with Pma


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Complex Structure of Sars-Cov 3C-Like Protease with Pma within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg601 b:35.2 occ:1.00 C2 A:BNZ602 2.2 31.1 1.0 SG A:CYS44 2.5 30.7 1.0 OH A:TYR54 2.6 33.8 1.0 C3 A:BNZ602 3.1 31.6 1.0 C1 A:BNZ602 3.2 32.1 1.0 CB A:CYS44 3.3 32.4 1.0 SD A:MET49 3.5 43.4 1.0 CB A:HIS41 3.6 30.3 1.0 CZ A:TYR54 3.7 32.4 1.0 O A:ASP187 4.1 28.2 1.0 CG A:PRO52 4.2 35.8 1.0 CE2 A:TYR54 4.3 32.9 1.0 CA A:MET49 4.3 39.4 1.0 CA A:HIS41 4.4 29.4 1.0 C6 A:BNZ602 4.5 30.7 1.0 CE A:MET49 4.5 47.2 1.0 C4 A:BNZ602 4.5 30.9 1.0 O A:MET49 4.6 39.1 1.0 O A:HIS41 4.6 29.5 1.0 CB A:PRO52 4.6 36.6 1.0 CG A:HIS41 4.7 32.4 1.0 CE1 A:TYR54 4.8 33.3 1.0 CA A:CYS44 4.8 32.1 1.0 C A:ASP187 4.9 28.1 1.0 O A:HOH1149 4.9 53.3 1.0 N A:MET49 4.9 38.8 1.0 CG A:MET49 4.9 41.4 1.0 O A:ASP48 4.9 39.6 1.0 CA A:ARG188 4.9 33.1 1.0 CB A:MET49 5.0 40.0 1.0 C A:MET49 5.0 39.1 1.0

C.C.Lee, C.J.Kuo, M.F.Hsu, P.H.Liang, J.M.Fang, J.J.Shie, A.H.Wang. Structural Basis of Mercury- and Zinc-Conjugated Complexes As Sars-Cov 3C-Like Protease Inhibitors. Febs Lett. V. 581 5454 2007.
ISSN: ISSN 0014-5793
PubMed: 17981158
DOI: 10.1016/J.FEBSLET.2007.10.048