Mercury in PDB 6sbh: Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide., PDB code: 6sbh was solved by S.Gloeckner, K.Ngo, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.93 / 0.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.294, 41.530, 72.165, 90.00, 104.52, 90.00
R / Rfree (%)	12 / 13.4

The structure of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide. (pdb code 6sbh). 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 4- Pentylbenzenesulfonamide., PDB code: 6sbh:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.


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 4- Pentylbenzenesulfonamide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg302 b:9.1 occ:0.20 SG A:CYS206 1.2 7.3 0.7 HG A:BE7303 1.3 7.7 0.6 HB3 A:CYS206 1.6 9.1 0.1 HB3 A:CYS206 2.0 9.2 0.2 O A:HOH555 2.4 22.5 1.0 SG A:CYS206 2.4 8.2 0.2 CB A:CYS206 2.6 7.7 0.2 CB A:CYS206 2.6 7.6 0.1 CB A:CYS206 2.8 6.7 0.7 HB3 A:CYS206 3.1 8.0 0.7 HB2 A:CYS206 3.1 9.1 0.1 O A:VAL135 3.1 10.5 1.0 HB3 A:LEU204 3.3 8.8 1.0 O A:GLN137 3.3 7.7 1.0 HA A:CYS206 3.3 7.0 0.7 HB2 A:CYS206 3.4 9.2 0.2 H A:GLN137 3.4 10.2 0.5 H A:GLN137 3.4 10.2 0.5 C5 A:BE7303 3.4 8.0 0.6 CA A:CYS206 3.5 5.8 0.7 SG A:CYS206 3.5 8.4 0.1 CA A:CYS206 3.5 6.9 0.2 CA A:CYS206 3.5 6.8 0.1 HA A:CYS206 3.5 8.2 0.1 HB2 A:CYS206 3.5 8.0 0.7 HG A:CYS206 3.5 10.1 0.1 HA A:CYS206 3.5 8.3 0.2 C A:VAL135 3.6 8.8 1.0 HA A:VAL135 3.6 10.9 1.0 N A:CYS206 3.6 6.7 0.2 N A:CYS206 3.7 6.6 0.1 N A:CYS206 3.7 6.0 0.7 N A:GLN137 3.7 8.5 1.0 C A:GLU205 3.7 6.5 1.0 O A:GLU205 3.8 7.6 1.0 O A:HOH549 3.8 14.5 1.0 HA A:GLN136 3.8 11.1 0.5 HA A:GLN136 3.9 11.8 0.5 C A:GLN137 3.9 7.5 1.0 H A:GLU205 4.0 7.4 1.0 H A:CYS206 4.0 8.0 0.2 C A:GLN136 4.1 9.4 0.5 H A:CYS206 4.1 7.9 0.1 C4 A:BE7303 4.1 8.9 0.6 C A:GLN136 4.1 8.9 0.5 N A:GLU205 4.1 6.2 1.0 N A:GLN136 4.1 8.9 0.5 N A:GLN136 4.1 8.6 0.5 CA A:VAL135 4.1 9.1 1.0 CB A:LEU204 4.2 7.4 1.0 H A:CYS206 4.2 7.2 0.7 CA A:GLN136 4.2 9.9 0.5 CA A:GLN136 4.2 9.2 0.5 HA A:PRO138 4.3 10.2 0.4 C6 A:BE7303 4.4 8.9 0.6 HB A:VAL135 4.4 12.3 1.0 HD13 A:LEU204 4.4 12.8 1.0 HB2 A:LEU204 4.4 8.8 1.0 HA A:PRO138 4.4 9.8 0.6 CA A:GLN137 4.4 7.9 1.0 C A:LEU204 4.5 5.9 1.0 CA A:GLU205 4.6 6.5 1.0 HD22 A:LEU204 4.6 13.2 1.0 O A:HOH595 4.6 34.7 1.0 O A:ALA134 4.6 7.8 1.0 N A:PRO138 4.8 7.9 0.6 N A:PRO138 4.8 8.2 0.4 H A:GLN136 4.8 10.7 0.5 H A:GLN136 4.8 10.4 0.5 O A:GLN136 4.8 10.0 0.5 CB A:VAL135 4.9 10.2 1.0 C A:CYS206 4.9 6.3 0.2 C A:CYS206 4.9 6.3 0.1 CA A:LEU204 4.9 6.5 1.0 C A:CYS206 4.9 5.7 0.7 HA A:GLN137 4.9 9.5 1.0 O A:GLN136 4.9 9.1 0.5 CA A:PRO138 5.0 8.5 0.4

Mercury binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.


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 4- Pentylbenzenesulfonamide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg303 b:7.7 occ:0.62 HG A:BE7303 0.0 7.7 0.6 HG A:HG302 1.3 9.1 0.2 C5 A:BE7303 2.2 8.0 0.6 HB3 A:CYS206 2.2 9.1 0.1 HB3 A:CYS206 2.3 9.2 0.2 SG A:CYS206 2.3 7.3 0.7 O A:HOH555 2.8 22.5 1.0 O A:GLN137 3.0 7.7 1.0 O A:GLU205 3.0 7.6 1.0 HA A:CYS206 3.0 7.0 0.7 CB A:CYS206 3.1 7.7 0.2 C6 A:BE7303 3.1 8.9 0.6 C4 A:BE7303 3.1 8.9 0.6 CB A:CYS206 3.1 7.6 0.1 HA A:CYS206 3.2 8.2 0.1 HA A:CYS206 3.2 8.3 0.2 HA A:PRO138 3.3 10.2 0.4 HA A:PRO138 3.3 9.8 0.6 C A:GLU205 3.4 6.5 1.0 C A:GLN137 3.4 7.5 1.0 CB A:CYS206 3.4 6.7 0.7 SG A:CYS206 3.5 8.2 0.2 CA A:CYS206 3.5 6.9 0.2 CA A:CYS206 3.5 6.8 0.1 CA A:CYS206 3.5 5.8 0.7 HB2 A:CYS206 3.6 9.1 0.1 HB3 A:CYS206 3.6 8.0 0.7 N A:CYS206 3.6 6.7 0.2 N A:CYS206 3.7 6.6 0.1 N A:CYS206 3.7 6.0 0.7 H A:GLN137 3.7 10.2 0.5 H A:GLN137 3.7 10.2 0.5 O A:HOH549 3.8 14.5 1.0 N A:GLN137 3.8 8.5 1.0 HB2 A:CYS206 3.9 9.2 0.2 N A:PRO138 3.9 7.9 0.6 N A:PRO138 3.9 8.2 0.4 H A:GLU205 4.0 7.4 1.0 CA A:PRO138 4.0 8.5 0.4 CA A:PRO138 4.0 8.2 0.6 CA A:GLN137 4.1 7.9 1.0 C A:GLN136 4.2 9.4 0.5 HB3 A:LEU204 4.2 8.8 1.0 HB2 A:CYS206 4.2 8.0 0.7 N A:GLU205 4.2 6.2 1.0 C A:GLN136 4.2 8.9 0.5 H A:CYS206 4.2 8.0 0.2 O A:VAL135 4.3 10.5 1.0 H A:CYS206 4.3 7.9 0.1 CA A:GLU205 4.3 6.5 1.0 HA A:GLN136 4.4 11.1 0.5 H A:CYS206 4.4 7.2 0.7 C3 A:BE7303 4.4 9.2 0.6 C7 A:BE7303 4.4 9.3 0.6 HA A:GLN136 4.4 11.8 0.5 SG A:CYS206 4.4 8.4 0.1 HG A:CYS206 4.4 10.1 0.1 HA A:GLN137 4.5 9.5 1.0 HB2 A:GLU205 4.5 8.1 1.0 O A:HOH595 4.6 34.7 1.0 O A:GLN136 4.6 10.0 0.5 C A:VAL135 4.6 8.8 1.0 HD3 A:PRO138 4.7 10.1 0.6 CA A:GLN136 4.7 9.9 0.5 HA A:VAL135 4.7 10.9 1.0 HB3 A:PRO138 4.7 11.5 0.4 CA A:GLN136 4.7 9.2 0.5 O A:GLN136 4.7 9.1 0.5 HD3 A:PRO138 4.8 10.7 0.4 CD A:PRO138 4.8 8.4 0.6 C A:PRO138 4.9 7.3 0.6 O A:HOH592 4.9 25.8 1.0 HG3 A:PRO138 4.9 10.5 0.6 C2 A:BE7303 4.9 9.4 0.6 N A:GLN136 4.9 8.9 0.5 CB A:GLU205 4.9 6.8 1.0 N A:GLN136 4.9 8.6 0.5 CD A:PRO138 5.0 8.9 0.4 C A:CYS206 5.0 5.7 0.7 C A:CYS206 5.0 6.3 0.2 C A:CYS206 5.0 6.3 0.1 C A:LEU204 5.0 5.9 1.0 C A:PRO138 5.0 7.7 0.4 CB A:PRO138 5.0 9.6 0.4

S.Glockner, K.Ngo, C.P.Sager, T.Hufner-Wulsdorf, A.Heine, G.Klebe. Conformational Changes in Alkyl Chains Determine the Thermodynamic and Kinetic Binding Profiles of Carbonic Anhydrase Inhibitors. Acs Chem.Biol. V. 15 675 2020.
ISSN: ESSN 1554-8937
PubMed: 32027480
DOI: 10.1021/ACSCHEMBIO.9B00895