Mercury in PDB 2geh: N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors

All present enzymatic activity of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors:
4.2.1.1;

The structure of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors, PDB code: 2geh was solved by C.Temperini, A.Innocenti, A.Scozzafava, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.201, 41.453, 72.268, 90.00, 104.40, 90.00
R / Rfree (%)	19.9 / 22.9

The structure of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors (pdb code 2geh). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors, PDB code: 2geh:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg263 b:13.8 occ:1.00 SG A:CYS206 2.1 6.2 1.0 O A:GLN137 2.9 7.0 1.0 O A:GLU205 3.2 4.6 1.0 CB A:CYS206 3.2 3.6 1.0 C A:GLN137 3.3 7.0 1.0 O A:HOH460 3.4 17.6 1.0 C A:GLU205 3.4 4.6 1.0 CA A:CYS206 3.4 3.8 1.0 N A:CYS206 3.6 3.6 1.0 N A:GLN137 3.8 8.4 1.0 N A:PRO138 3.9 6.5 1.0 O A:VAL135 4.0 7.1 1.0 O A:HOH390 4.0 13.4 1.0 CA A:PRO138 4.0 6.4 1.0 CA A:GLN137 4.1 7.8 1.0 C A:GLN136 4.1 9.3 1.0 N A:GLU205 4.2 5.5 1.0 CA A:GLU205 4.3 5.0 1.0 C A:VAL135 4.4 6.5 1.0 O A:GLN136 4.5 9.9 1.0 CA A:GLN136 4.7 9.6 1.0 O A:HOH449 4.7 29.2 1.0 N A:GLN136 4.8 8.1 1.0 C A:LEU204 4.9 5.8 1.0 C A:CYS206 4.9 2.8 1.0 CB A:LEU204 4.9 6.0 1.0 CB A:GLU205 4.9 5.2 1.0 C A:PRO138 5.0 6.4 1.0

Mercury binding site 2 out of 2 in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg264 b:38.7 occ:1.00 CD2 A:HIS64 2.3 11.8 1.0 O A:ASN62 3.0 7.9 1.0 CG A:HIS64 3.1 10.6 1.0 N A:HIS64 3.4 7.8 1.0 CB A:HIS64 3.4 8.8 1.0 NE2 A:HIS64 3.5 13.7 1.0 C A:GLY63 3.6 7.5 1.0 O A:HOH469 3.8 11.5 1.0 C A:ASN62 3.9 7.5 1.0 CA A:GLY63 3.9 7.0 1.0 CA A:HIS64 4.0 8.4 1.0 O A:HOH466 4.1 26.1 1.0 OD1 A:ASN62 4.2 3.8 1.0 CZ2 A:TRP5 4.2 12.1 1.0 O A:GLY63 4.2 7.3 1.0 N A:GLY63 4.3 7.1 1.0 ND1 A:HIS64 4.4 14.0 1.0 CE1 A:HIS64 4.5 14.2 1.0 CH2 A:TRP5 4.6 11.1 1.0 O A:HOH420 4.6 18.8 1.0 CG A:ASN62 4.7 6.3 1.0 CE2 A:TRP5 4.8 11.8 1.0 CB A:ASN62 4.9 6.9 1.0

C.Temperini, A.Innocenti, A.Scozzafava, C.T.Supuran. N-Hydroxyurea-A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors. Bioorg.Med.Chem.Lett. V. 16 4316 2006.
ISSN: ISSN 0960-894X
PubMed: 16759856
DOI: 10.1016/J.BMCL.2006.05.068