Mercury in PDB 6roe: Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6roe was solved by S.Gloeckner, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.63 / 0.94
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.364, 41.401, 72.278, 90.00, 104.53, 90.00
R / Rfree (%)	11 / 11.9

The structure of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide also contains other interesting chemical elements:

Fluorine	(F)	6 atoms
Zinc	(Zn)	1 atom

The binding sites of Mercury atom in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide (pdb code 6roe). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6roe:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg305 b:8.5 occ:0.20 SG A:CYS206 1.3 7.0 0.8 HG A:BE7306 1.3 7.3 0.6 HB3 A:CYS206 1.7 9.3 0.1 HB3 A:CYS206 2.0 8.7 0.2 SG A:CYS206 2.4 6.4 0.2 O A:HOH537 2.4 16.5 1.0 CB A:CYS206 2.6 7.2 0.2 CB A:CYS206 2.7 7.8 0.1 CB A:CYS206 2.8 5.9 0.8 HB3 A:CYS206 3.1 7.1 0.8 O A:VAL135 3.1 9.7 1.0 HB2 A:CYS206 3.1 9.3 0.1 HB3 A:LEU204 3.2 8.9 1.0 O A:GLN137 3.3 7.4 1.0 HB2 A:CYS206 3.3 8.7 0.2 HA A:CYS206 3.3 6.1 0.8 H A:GLN137 3.4 8.9 0.5 H A:GLN137 3.5 8.9 0.5 C5 A:BE7306 3.5 8.1 0.6 HA A:CYS206 3.5 8.2 0.1 CA A:CYS206 3.5 6.9 0.1 CA A:CYS206 3.5 5.1 0.8 CA A:CYS206 3.5 6.8 0.2 HB2 A:CYS206 3.5 7.1 0.8 C A:VAL135 3.5 8.4 1.0 HA A:VAL135 3.5 9.8 1.0 HA A:CYS206 3.6 8.2 0.2 SG A:CYS206 3.6 7.3 0.1 N A:CYS206 3.6 6.5 0.2 N A:CYS206 3.7 6.4 0.1 HG A:CYS206 3.7 8.8 0.1 N A:CYS206 3.7 5.3 0.8 N A:GLN137 3.7 7.4 1.0 C A:GLU205 3.7 6.0 1.0 O A:GLU205 3.8 7.5 1.0 O A:HOH546 3.8 13.4 1.0 HA A:GLN136 3.9 10.4 0.5 HA A:GLN136 3.9 10.5 0.5 C A:GLN137 3.9 6.8 1.0 H A:GLU205 3.9 7.2 1.0 H A:CYS206 4.0 7.8 0.2 C A:GLN136 4.0 8.0 0.5 CA A:VAL135 4.1 8.1 1.0 N A:GLN136 4.1 8.3 0.5 N A:GLN136 4.1 8.3 0.5 N A:GLU205 4.1 6.0 1.0 C A:GLN136 4.1 8.0 0.5 H A:CYS206 4.1 7.7 0.1 C6 A:BE7306 4.1 8.7 0.6 CB A:LEU204 4.2 7.5 1.0 H A:CYS206 4.2 6.4 0.8 CA A:GLN136 4.2 8.7 0.5 CA A:GLN136 4.2 8.7 0.5 HA A:PRO138 4.3 9.2 0.5 HB A:VAL135 4.3 11.3 1.0 HA A:PRO138 4.4 9.4 0.5 HB2 A:LEU204 4.4 8.9 1.0 C4 A:BE7306 4.4 8.2 0.6 HD13 A:LEU204 4.4 12.7 1.0 CA A:GLN137 4.4 7.1 1.0 C A:LEU204 4.5 5.7 1.0 CA A:GLU205 4.6 5.7 1.0 O A:ALA134 4.6 7.4 1.0 HD22 A:LEU204 4.6 13.5 1.0 N A:PRO138 4.7 7.1 0.5 O A:GLN136 4.7 8.8 0.5 N A:PRO138 4.8 7.0 0.5 H A:GLN136 4.8 10.0 0.5 H A:GLN136 4.8 10.0 0.5 CB A:VAL135 4.8 9.4 1.0 CA A:LEU204 4.9 6.3 1.0 C A:CYS206 4.9 6.2 0.2 HA A:GLN137 4.9 8.6 1.0 C A:CYS206 4.9 6.1 0.1 O A:GLN136 4.9 8.3 0.5 C A:CYS206 4.9 5.3 0.8 CA A:PRO138 5.0 7.9 0.5 CA A:PRO138 5.0 7.7 0.5

Mercury binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg306 b:7.3 occ:0.64 HG A:BE7306 0.0 7.3 0.6 HG A:HG305 1.3 8.5 0.2 C5 A:BE7306 2.2 8.1 0.6 HB3 A:CYS206 2.2 8.7 0.2 SG A:CYS206 2.3 7.0 0.8 HB3 A:CYS206 2.3 9.3 0.1 O A:HOH537 2.9 16.5 1.0 O A:GLN137 3.0 7.4 1.0 O A:GLU205 3.0 7.5 1.0 CB A:CYS206 3.0 7.2 0.2 HA A:CYS206 3.1 6.1 0.8 C4 A:BE7306 3.1 8.2 0.6 C6 A:BE7306 3.1 8.7 0.6 HA A:CYS206 3.2 8.2 0.1 CB A:CYS206 3.2 7.8 0.1 HA A:PRO138 3.2 9.2 0.5 HA A:CYS206 3.3 8.2 0.2 HA A:PRO138 3.3 9.4 0.5 C A:GLU205 3.4 6.0 1.0 C A:GLN137 3.4 6.8 1.0 CB A:CYS206 3.4 5.9 0.8 SG A:CYS206 3.5 6.4 0.2 CA A:CYS206 3.5 6.8 0.2 CA A:CYS206 3.5 6.9 0.1 CA A:CYS206 3.5 5.1 0.8 HB3 A:CYS206 3.6 7.1 0.8 N A:CYS206 3.6 6.5 0.2 HB2 A:CYS206 3.6 9.3 0.1 N A:CYS206 3.7 6.4 0.1 N A:CYS206 3.7 5.3 0.8 H A:GLN137 3.7 8.9 0.5 O A:HOH546 3.8 13.4 1.0 H A:GLN137 3.8 8.9 0.5 N A:GLN137 3.8 7.4 1.0 HB2 A:CYS206 3.8 8.7 0.2 N A:PRO138 3.9 7.1 0.5 N A:PRO138 3.9 7.0 0.5 H A:GLU205 4.0 7.2 1.0 CA A:PRO138 4.0 7.7 0.5 CA A:PRO138 4.0 7.9 0.5 CA A:GLN137 4.1 7.1 1.0 C A:GLN136 4.2 8.0 0.5 HB3 A:LEU204 4.2 8.9 1.0 N A:GLU205 4.2 6.0 1.0 HB2 A:CYS206 4.2 7.1 0.8 H A:CYS206 4.3 7.8 0.2 C A:GLN136 4.3 8.0 0.5 O A:VAL135 4.3 9.7 1.0 CA A:GLU205 4.3 5.7 1.0 H A:CYS206 4.3 7.7 0.1 H A:CYS206 4.4 6.4 0.8 HA A:GLN136 4.4 10.4 0.5 C7 A:BE7306 4.4 9.0 0.6 C3 A:BE7306 4.4 9.1 0.6 HA A:GLN136 4.4 10.5 0.5 HA A:GLN137 4.4 8.6 1.0 HB2 A:GLU205 4.5 7.7 1.0 SG A:CYS206 4.5 7.3 0.1 O A:GLN136 4.6 8.8 0.5 HG A:CYS206 4.6 8.8 0.1 C A:VAL135 4.6 8.4 1.0 HD3 A:PRO138 4.7 9.1 0.5 HA A:VAL135 4.7 9.8 1.0 CA A:GLN136 4.7 8.7 0.5 HB3 A:PRO138 4.8 11.0 0.5 CA A:GLN136 4.8 8.7 0.5 O A:GLN136 4.8 8.3 0.5 CD A:PRO138 4.8 7.5 0.5 HD3 A:PRO138 4.8 9.9 0.5 C A:PRO138 4.8 7.0 0.5 HG3 A:PRO138 4.9 10.1 0.5 CB A:GLU205 4.9 6.4 1.0 N A:GLN136 4.9 8.3 0.5 C2 A:BE7306 4.9 9.2 0.6 N A:GLN136 4.9 8.3 0.5 C A:PRO138 5.0 7.0 0.5 C A:LEU204 5.0 5.7 1.0 O A:HOH579 5.0 29.1 1.0 C A:CYS206 5.0 6.1 0.1 C A:CYS206 5.0 5.3 0.8 C A:CYS206 5.0 6.2 0.2 CD A:PRO138 5.0 8.2 0.5

S.Glockner, K.Ngo, B.Wagner, A.Heine, G.Klebe. The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32230853
DOI: 10.3390/BIOM10040509