Mercury in PDB 4frc: Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide

All present enzymatic activity of Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide:
4.2.1.1;

The structure of Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide, PDB code: 4frc 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 (°)	42.179, 41.584, 72.296, 90.00, 104.20, 90.00
R / Rfree (%)	12.3 / 13.9

The structure of Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide 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'-Sulfamoylpyrrolidine-1- Carboximidamide (pdb code 4frc). 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'-Sulfamoylpyrrolidine-1- Carboximidamide, PDB code: 4frc:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide


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'-Sulfamoylpyrrolidine-1- Carboximidamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg301 b:7.3 occ:0.68 HG A:MBO301 0.0 7.3 0.7 HG A:MBO301 1.2 10.0 0.3 CE1 A:MBO301 2.1 7.7 0.7 SG A:CYS206 2.3 6.2 0.7 O A:GLN137 3.0 7.4 1.0 O A:HOH436 3.0 15.2 1.0 CE6 A:MBO301 3.0 9.3 0.7 O A:GLU205 3.1 7.4 1.0 CE2 A:MBO301 3.1 10.4 0.7 SG A:CYS206 3.2 8.2 0.3 CB A:CYS206 3.2 5.8 0.7 C A:GLN137 3.4 6.9 1.0 C A:GLU205 3.4 6.0 1.0 CA A:CYS206 3.5 6.2 0.7 CA A:CYS206 3.5 3.6 0.3 N A:CYS206 3.6 5.2 1.0 CB A:CYS206 3.6 6.4 0.3 N A:GLN137 3.7 7.8 1.0 O A:HOH437 3.8 13.6 1.0 N A:PRO138 3.9 7.7 1.0 CA A:PRO138 4.0 8.0 1.0 CA A:GLN137 4.1 7.5 1.0 O A:VAL135 4.1 9.9 1.0 N A:GLU205 4.2 5.8 1.0 C A:GLN136 4.2 8.8 1.0 CA A:GLU205 4.3 5.9 1.0 CE5 A:MBO301 4.4 8.7 0.7 CE3 A:MBO301 4.4 9.6 0.7 C A:VAL135 4.6 8.0 1.0 CA A:GLN136 4.7 8.6 1.0 O A:GLN136 4.8 10.5 1.0 O A:HOH675 4.8 34.2 1.0 C A:LEU204 4.9 5.7 1.0 N A:GLN136 4.9 8.4 1.0 CB A:GLU205 4.9 6.2 1.0 C A:CYS206 4.9 5.2 1.0 CD A:PRO138 4.9 9.6 1.0 CE4 A:MBO301 4.9 10.1 0.7 CB A:LEU204 5.0 8.2 1.0 C A:PRO138 5.0 7.7 1.0

Mercury binding site 2 out of 2 in the Carbonic Anhydrase II in Complex with N'-Sulfamoylpyrrolidine-1- Carboximidamide


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'-Sulfamoylpyrrolidine-1- Carboximidamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg301 b:10.0 occ:0.32 HG A:MBO301 0.0 10.0 0.3 HG A:MBO301 1.2 7.3 0.7 SG A:CYS206 1.4 6.2 0.7 SG A:CYS206 2.3 8.2 0.3 O A:HOH436 2.5 15.2 1.0 CB A:CYS206 2.8 5.8 0.7 O A:VAL135 3.1 9.9 1.0 CE1 A:MBO301 3.2 7.7 0.7 CB A:CYS206 3.2 6.4 0.3 O A:GLN137 3.3 7.4 1.0 CA A:CYS206 3.5 6.2 0.7 CA A:CYS206 3.5 3.6 0.3 C A:VAL135 3.6 8.0 1.0 N A:GLN137 3.6 7.8 1.0 N A:CYS206 3.7 5.2 1.0 C A:GLU205 3.8 6.0 1.0 O A:GLU205 3.8 7.4 1.0 O A:HOH437 3.8 13.6 1.0 C A:GLN137 3.9 6.9 1.0 CE2 A:MBO301 4.0 10.4 0.7 N A:GLU205 4.1 5.8 1.0 CB A:LEU204 4.1 8.2 1.0 C A:GLN136 4.1 8.8 1.0 N A:GLN136 4.2 8.4 1.0 CE6 A:MBO301 4.2 9.3 0.7 CA A:VAL135 4.2 7.8 1.0 CA A:GLN136 4.3 8.6 1.0 CA A:GLN137 4.4 7.5 1.0 C A:LEU204 4.5 5.7 1.0 CA A:GLU205 4.5 5.9 1.0 O A:ALA134 4.7 7.1 1.0 N A:PRO138 4.7 7.7 1.0 CA A:LEU204 4.8 6.8 1.0 O A:GLN136 4.9 10.5 1.0 CB A:VAL135 4.9 9.0 1.0 C A:CYS206 4.9 5.2 1.0 CA A:PRO138 5.0 8.0 1.0

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