Mercury in PDB 6say: Human Carbonic Anhydrase II in Complex with Fragment.

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

The structure of Human Carbonic Anhydrase II in Complex with Fragment., PDB code: 6say 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)	34.93 / 0.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.390, 41.508, 72.214, 90.00, 104.68, 90.00
R / Rfree (%)	12.2 / 13.8

The structure of Human Carbonic Anhydrase II in Complex with Fragment. 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 Fragment. (pdb code 6say). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Human Carbonic Anhydrase II in Complex with Fragment., PDB code: 6say:
Jump to Mercury binding site number: 1; 2; 3; 4;

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


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 Fragment. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg302 b:22.8 occ:0.27 HG A:BE7305 0.9 7.6 0.7 SG A:CYS206 1.6 6.4 0.7 HB3 A:CYS206 2.0 15.2 0.3 O A:HOH493 2.6 13.8 1.0 CB A:CYS206 2.7 12.7 0.3 SG A:CYS206 2.8 16.2 0.3 CB A:CYS206 2.9 5.6 0.7 C5 A:BE7305 3.0 7.3 0.7 O A:GLN137 3.0 7.1 0.6 H A:GLN137 3.1 9.9 0.6 HB3 A:CYS206 3.2 6.7 0.7 HA A:CYS206 3.2 6.6 0.7 O A:GLN137 3.3 7.1 0.4 H A:GLN137 3.3 9.7 0.4 O A:VAL135 3.4 10.5 1.0 HB2 A:CYS206 3.5 15.2 0.3 CA A:CYS206 3.5 5.5 0.7 HA A:CYS206 3.5 11.2 0.3 CA A:CYS206 3.5 9.3 0.3 N A:GLN137 3.5 8.2 0.6 N A:GLN137 3.6 8.1 0.4 O A:GLU205 3.6 8.4 1.0 C A:GLU205 3.7 6.8 1.0 N A:CYS206 3.7 8.0 0.3 C A:GLN137 3.7 7.2 0.6 HB3 A:LEU204 3.7 13.3 0.4 HB2 A:CYS206 3.7 6.7 0.7 C A:VAL135 3.7 8.6 1.0 C4 A:BE7305 3.7 9.3 0.7 N A:CYS206 3.7 5.7 0.7 C A:GLN137 3.8 7.5 0.4 HA A:VAL135 3.8 10.2 1.0 HA A:GLN136 3.8 11.2 0.6 HB3 A:LEU204 3.9 16.2 0.6 O A:HOH545 3.9 18.3 1.0 HA A:GLN136 3.9 10.9 0.4 C A:GLN136 3.9 8.3 0.4 C6 A:BE7305 4.0 7.7 0.7 H A:GLU205 4.0 9.8 0.6 H A:GLU205 4.0 9.8 0.4 C A:GLN136 4.1 8.4 0.6 HA A:PRO138 4.1 9.8 1.0 H A:CYS206 4.2 9.6 0.3 N A:GLN136 4.2 8.8 0.6 N A:GLN136 4.2 8.7 0.4 N A:GLU205 4.2 8.2 1.0 CA A:GLN137 4.2 7.9 0.6 CA A:GLN136 4.2 9.4 0.6 CA A:GLN136 4.2 9.1 0.4 CA A:GLN137 4.3 8.1 0.4 H A:CYS206 4.3 6.8 0.7 CA A:VAL135 4.3 8.5 1.0 N A:PRO138 4.5 7.4 1.0 CA A:GLU205 4.5 7.3 1.0 O A:GLN136 4.6 9.0 0.4 HB A:VAL135 4.6 11.2 1.0 HA A:GLN137 4.7 9.5 0.6 CB A:LEU204 4.7 11.1 0.4 HA A:GLN137 4.7 9.7 0.4 O A:ALA134 4.7 8.3 1.0 HD13 A:LEU204 4.7 15.1 0.4 HB2 A:GLU205 4.8 10.0 1.0 C A:LEU204 4.8 8.8 0.4 HD22 A:LEU204 4.8 15.4 0.4 CB A:LEU204 4.8 13.5 0.6 CA A:PRO138 4.8 8.1 1.0 C A:LEU204 4.8 8.4 0.6 H A:GLN136 4.8 10.6 0.6 H A:GLN136 4.8 10.4 0.4 O A:HOH599 4.8 33.9 1.0 O A:GLN136 4.9 9.1 0.6 C A:CYS206 4.9 7.6 0.3 C A:CYS206 4.9 5.8 0.7

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


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 Fragment. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg303 b:11.5 occ:0.17 CD2 A:HIS64 1.1 9.6 0.4 NE2 A:HIS64 1.2 10.9 0.4 HD2 A:HIS64 1.5 11.5 0.4 ND1 A:HIS64 2.2 13.6 0.6 CG A:HIS64 2.2 10.3 0.4 CE1 A:HIS64 2.2 11.2 0.4 ND1 A:HIS64 2.6 11.4 0.4 O A:ASN62 2.8 10.7 0.6 HE1 A:HIS64 3.0 13.4 0.4 HB3 A:HIS64 3.0 15.3 0.6 O A:ASN62 3.0 10.5 0.4 CE1 A:HIS64 3.1 14.6 0.6 CG A:HIS64 3.2 13.0 0.6 HE1 A:HIS64 3.2 17.6 0.6 HD1 A:HIS64 3.5 13.7 0.4 HE1 A:HIS4 3.5 27.0 1.0 CB A:HIS64 3.5 10.2 0.4 CB A:HIS64 3.5 12.7 0.6 N A:HIS64 3.6 10.3 0.6 H A:HIS64 3.6 12.4 0.6 HA3 A:GLY63 3.6 12.2 1.0 HB2 A:HIS64 3.7 12.3 0.4 N A:HIS64 3.7 9.9 0.4 C A:GLY63 3.7 10.1 1.0 H A:HIS64 3.8 11.8 0.4 C A:ASN62 3.9 9.4 0.6 HZ2 A:TRP5 4.0 14.3 1.0 C A:ASN62 4.0 9.7 0.4 CA A:GLY63 4.1 10.1 1.0 O A:GLY63 4.1 11.2 1.0 CA A:HIS64 4.2 11.2 0.6 CZ2 A:TRP5 4.2 11.9 1.0 CA A:HIS64 4.2 10.0 0.4 HB3 A:HIS64 4.2 12.3 0.4 CE1 A:HIS4 4.2 22.5 1.0 NE2 A:HIS64 4.3 15.5 0.6 CD2 A:HIS64 4.3 14.8 0.6 CG A:ASN62 4.3 10.9 0.4 OD1 A:ASN62 4.4 8.7 0.6 HB2 A:HIS64 4.4 15.3 0.6 OD1 A:ASN62 4.4 9.9 0.4 ND2 A:ASN62 4.4 11.7 0.4 N A:GLY63 4.4 9.4 1.0 HB2 A:ASN62 4.4 11.3 0.6 HD21 A:ASN62 4.5 14.0 0.4 HA A:HIS64 4.5 12.0 0.4 HB2 A:ASN62 4.5 12.4 0.4 CH2 A:TRP5 4.6 11.6 1.0 HA A:HIS64 4.6 13.4 0.6 HH2 A:TRP5 4.7 13.9 1.0 CE2 A:TRP5 4.7 10.8 1.0 HD22 A:ASN62 4.7 14.0 0.4 CG A:ASN62 4.8 8.9 0.6 CB A:ASN62 4.9 10.4 0.4 HD1 A:HIS4 4.9 26.0 1.0 ND1 A:HIS4 4.9 21.6 1.0 O A:HOH483 4.9 17.5 1.0 CB A:ASN62 5.0 9.4 0.6 HA2 A:GLY63 5.0 12.2 1.0

Mercury binding site 3 out of 4 in the Human Carbonic Anhydrase II in Complex with Fragment.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Human Carbonic Anhydrase II in Complex with Fragment. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg304 b:25.9 occ:0.19 OD1 A:ASP72 3.1 15.8 1.0 O A:PHE70 3.3 10.6 1.0 H A:ASP72 3.3 14.4 0.5 H A:ASP72 3.4 14.4 0.5 HA A:ASP71 3.6 14.6 0.5 HA A:ASP71 3.7 13.0 0.5 CG A:ASP72 3.9 13.4 1.0 HD12 A:LEU57 4.1 19.4 1.0 N A:ASP72 4.2 12.0 1.0 HG13 A:ILE91 4.2 12.2 1.0 C A:PHE70 4.3 9.4 1.0 OD2 A:ASP72 4.4 14.2 1.0 CA A:ASP71 4.5 12.2 0.5 HD11 A:LEU57 4.5 19.4 1.0 CA A:ASP71 4.5 10.8 0.5 CD1 A:LEU57 4.7 16.2 1.0 HD11 A:ILE91 4.8 14.4 1.0 C A:ASP71 4.8 10.8 0.5 N A:ASP71 4.9 10.2 0.5 N A:ASP71 4.9 10.8 0.5 HB3 A:ASP72 4.9 15.2 1.0 C A:ASP71 4.9 11.7 0.5 CB A:ASP72 4.9 12.6 1.0 HD13 A:LEU57 4.9 19.4 1.0 HB3 A:GLU69 4.9 13.6 0.4

Mercury binding site 4 out of 4 in the Human Carbonic Anhydrase II in Complex with Fragment.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Human Carbonic Anhydrase II in Complex with Fragment. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg305 b:7.6 occ:0.73 HG A:BE7305 0.0 7.6 0.7 HG A:HG302 0.9 22.8 0.3 C5 A:BE7305 2.2 7.3 0.7 HB3 A:CYS206 2.2 15.2 0.3 SG A:CYS206 2.4 6.4 0.7 O A:GLN137 2.9 7.1 0.6 CB A:CYS206 3.0 12.7 0.3 O A:HOH493 3.0 13.8 1.0 HA A:CYS206 3.0 6.6 0.7 C6 A:BE7305 3.1 7.7 0.7 C4 A:BE7305 3.1 9.3 0.7 O A:GLU205 3.1 8.4 1.0 O A:GLN137 3.1 7.1 0.4 HA A:CYS206 3.2 11.2 0.3 C A:GLN137 3.3 7.2 0.6 CB A:CYS206 3.3 5.6 0.7 HA A:PRO138 3.4 9.8 1.0 H A:GLN137 3.4 9.9 0.6 C A:GLU205 3.4 6.8 1.0 C A:GLN137 3.4 7.5 0.4 SG A:CYS206 3.5 16.2 0.3 CA A:CYS206 3.5 9.3 0.3 CA A:CYS206 3.5 5.5 0.7 HB3 A:CYS206 3.5 6.7 0.7 H A:GLN137 3.6 9.7 0.4 N A:GLN137 3.6 8.2 0.6 N A:CYS206 3.7 8.0 0.3 N A:GLN137 3.7 8.1 0.4 N A:CYS206 3.7 5.7 0.7 HB2 A:CYS206 3.8 15.2 0.3 N A:PRO138 3.9 7.4 1.0 O A:HOH545 4.0 18.3 1.0 H A:GLU205 4.0 9.8 0.4 H A:GLU205 4.0 9.8 0.6 CA A:GLN137 4.0 7.9 0.6 C A:GLN136 4.1 8.3 0.4 CA A:PRO138 4.1 8.1 1.0 CA A:GLN137 4.1 8.1 0.4 O A:VAL135 4.2 10.5 1.0 HB2 A:CYS206 4.2 6.7 0.7 C A:GLN136 4.2 8.4 0.6 HA A:GLN136 4.2 11.2 0.6 H A:CYS206 4.3 9.6 0.3 N A:GLU205 4.3 8.2 1.0 HA A:GLN136 4.3 10.9 0.4 CA A:GLU205 4.4 7.3 1.0 C7 A:BE7305 4.4 7.7 0.7 C3 A:BE7305 4.4 9.1 0.7 HB2 A:GLU205 4.4 10.0 1.0 HA A:GLN137 4.4 9.5 0.6 HB3 A:LEU204 4.4 13.3 0.4 HA A:GLN137 4.4 9.7 0.4 H A:CYS206 4.4 6.8 0.7 C A:VAL135 4.5 8.6 1.0 O A:GLN136 4.5 9.0 0.4 HA A:VAL135 4.6 10.2 1.0 HB3 A:LEU204 4.6 16.2 0.6 CA A:GLN136 4.6 9.4 0.6 CA A:GLN136 4.6 9.1 0.4 HD3 A:PRO138 4.7 11.1 1.0 N A:GLN136 4.8 8.8 0.6 N A:GLN136 4.8 8.7 0.4 CB A:GLU205 4.8 8.3 1.0 O A:GLN136 4.9 9.1 0.6 C2 A:BE7305 4.9 8.7 0.7 HB3 A:PRO138 4.9 11.5 1.0 CD A:PRO138 4.9 9.3 1.0 C A:CYS206 4.9 5.8 0.7 C A:CYS206 5.0 7.6 0.3 O A:HOH599 5.0 33.9 1.0

S.Glockner, A.Heine, G.Klebe. A Proof-of-Concept Fragment Screening of A Hit-Validated 96-Compounds Library Against Human Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32235320
DOI: 10.3390/BIOM10040518