Mercury in PDB 4fu5: Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide

All present enzymatic activity of Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide:
4.2.1.1;

The structure of Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide, PDB code: 4fu5 was solved by A.Di Pizio, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 0.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.183, 41.532, 72.172, 90.00, 104.23, 90.00
R / Rfree (%)	12.4 / 15

The structure of Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide (pdb code 4fu5). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide, PDB code: 4fu5:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg301 b:6.9 occ:0.70 HG A:MBO301 0.0 6.9 0.7 HG A:MBO301 1.2 9.3 0.3 CE1 A:MBO301 2.1 7.9 0.7 SG A:CYS206 2.3 5.8 0.7 O A:GLN137 3.0 6.7 1.0 O A:HOH451 3.0 14.3 1.0 CE6 A:MBO301 3.0 8.2 0.7 O A:GLU205 3.1 6.9 1.0 CE2 A:MBO301 3.1 10.1 0.7 SG A:CYS206 3.2 8.1 0.3 CB A:CYS206 3.2 5.8 0.7 C A:GLU205 3.4 5.5 1.0 C A:GLN137 3.4 6.3 1.0 CA A:CYS206 3.5 5.2 0.7 CA A:CYS206 3.5 4.8 0.3 N A:CYS206 3.6 4.9 1.0 CB A:CYS206 3.7 5.7 0.3 N A:GLN137 3.7 7.3 1.0 O A:HOH424 3.8 12.2 1.0 N A:PRO138 3.9 6.9 1.0 CA A:PRO138 4.1 7.2 1.0 CA A:GLN137 4.1 6.9 1.0 N A:GLU205 4.1 5.8 1.0 O A:VAL135 4.2 9.5 1.0 C A:GLN136 4.2 7.8 1.0 CA A:GLU205 4.3 5.4 1.0 CE5 A:MBO301 4.4 8.4 0.7 CE3 A:MBO301 4.4 9.4 0.7 C A:VAL135 4.6 7.7 1.0 O A:GLN136 4.7 9.5 1.0 CA A:GLN136 4.7 8.6 1.0 O A:HOH616 4.8 33.5 1.0 C A:LEU204 4.8 5.4 1.0 N A:GLN136 4.9 8.0 1.0 CB A:GLU205 4.9 6.0 1.0 CE4 A:MBO301 4.9 9.6 0.7 CD A:PRO138 4.9 9.5 1.0 C A:CYS206 4.9 4.8 1.0 C A:PRO138 5.0 7.0 1.0 CB A:LEU204 5.0 8.2 1.0

Mercury binding site 2 out of 2 in the Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Carbonic Anhydrase II in Complex with N-[(2Z)-1,3-Oxazolidin-2- Ylidene]Sulfuric Diamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg301 b:9.3 occ:0.30 HG A:MBO301 0.0 9.3 0.3 HG A:MBO301 1.2 6.9 0.7 SG A:CYS206 1.4 5.8 0.7 SG A:CYS206 2.3 8.1 0.3 O A:HOH451 2.5 14.3 1.0 CB A:CYS206 2.8 5.8 0.7 O A:VAL135 3.2 9.5 1.0 CE1 A:MBO301 3.2 7.9 0.7 CB A:CYS206 3.2 5.7 0.3 O A:GLN137 3.3 6.7 1.0 CA A:CYS206 3.5 5.2 0.7 CA A:CYS206 3.5 4.8 0.3 C A:VAL135 3.6 7.7 1.0 N A:GLN137 3.7 7.3 1.0 N A:CYS206 3.7 4.9 1.0 C A:GLU205 3.7 5.5 1.0 O A:GLU205 3.8 6.9 1.0 O A:HOH424 3.8 12.2 1.0 C A:GLN137 3.9 6.3 1.0 CE2 A:MBO301 4.0 10.1 0.7 C A:GLN136 4.1 7.8 1.0 N A:GLU205 4.1 5.8 1.0 CB A:LEU204 4.2 8.2 1.0 N A:GLN136 4.2 8.0 1.0 CE6 A:MBO301 4.2 8.2 0.7 CA A:VAL135 4.2 7.2 1.0 CA A:GLN136 4.3 8.6 1.0 CA A:GLN137 4.4 6.9 1.0 C A:LEU204 4.5 5.4 1.0 CA A:GLU205 4.6 5.4 1.0 O A:ALA134 4.7 6.8 1.0 N A:PRO138 4.7 6.9 1.0 CA A:LEU204 4.8 6.3 1.0 O A:GLN136 4.8 9.5 1.0 CB A:VAL135 4.9 8.8 1.0 C A:CYS206 4.9 4.8 1.0 CA A:PRO138 5.0 7.2 1.0

A.Di Pizio, J.Schulze Wischeler, M.Haake, A.Heine, C.Supuran, G.Klebe. High Resolution Crystal Structures of Carbonic Anhzdrase II in Complex with Nonvel Sulfamide Binders To Be Published.