Zinc in PDB 3rts: Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide

All present enzymatic activity of Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide:
3.4.24.65;

The structure of Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide, PDB code: 3rts was solved by I.Bertini, V.Calderone, M.Fragai, C.Luchinat, M.Mori, C.Nativi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.99 / 1.81
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.643, 60.475, 54.162, 90.00, 115.15, 90.00
R / Rfree (%)	17 / 23.6

The structure of Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide (pdb code 3rts). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide, PDB code: 3rts:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn264 b:6.7 occ:1.00 NE2 A:HIS218 2.1 2.0 1.0 NE2 A:HIS222 2.1 2.3 1.0 NE2 A:HIS228 2.1 4.1 1.0 O3 A:KLG0 2.2 7.8 1.0 O4 A:KLG0 2.3 3.3 1.0 CD2 A:HIS218 2.9 2.0 1.0 C10 A:KLG0 3.0 7.6 1.0 CD2 A:HIS222 3.0 2.0 1.0 CE1 A:HIS228 3.0 2.5 1.0 N1 A:KLG0 3.0 7.2 1.0 CD2 A:HIS228 3.1 2.4 1.0 CE1 A:HIS218 3.1 2.0 1.0 CE1 A:HIS222 3.2 3.6 1.0 O A:HOH12 4.1 2.4 1.0 CG A:HIS218 4.1 2.1 1.0 ND1 A:HIS228 4.1 3.0 1.0 CG A:HIS222 4.2 2.3 1.0 ND1 A:HIS218 4.2 4.0 1.0 ND1 A:HIS222 4.2 3.2 1.0 CG A:HIS228 4.2 3.6 1.0 OE1 A:GLU219 4.3 2.2 1.0 C8 A:KLG0 4.4 11.1 1.0 C9 A:KLG0 4.4 7.8 1.0 O A:HOH41 4.8 8.9 1.0 CE A:MET236 4.9 4.8 1.0 N2 A:KLG0 5.0 9.9 1.0

Zinc binding site 2 out of 2 in the Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Mmp-12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2- Phenylethylsulfonamido)Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn265 b:8.6 occ:1.00 NE2 A:HIS183 1.9 7.9 1.0 OD1 A:ASP170 2.0 7.1 0.7 NE2 A:HIS168 2.0 2.5 1.0 ND1 A:HIS196 2.1 2.4 1.0 CE1 A:HIS183 2.7 8.8 1.0 CD2 A:HIS168 2.9 6.9 1.0 CG A:ASP170 2.9 10.8 0.7 CE1 A:HIS196 3.0 2.7 1.0 CG A:HIS196 3.1 2.0 1.0 CD2 A:HIS183 3.1 7.2 1.0 CE1 A:HIS168 3.1 5.6 1.0 OD2 A:ASP170 3.2 7.7 0.7 CB A:HIS196 3.4 3.3 1.0 ND1 A:HIS183 3.9 8.7 1.0 CG A:HIS168 4.1 8.0 1.0 CG A:HIS183 4.1 6.1 1.0 O A:HIS172 4.1 14.7 1.0 NE2 A:HIS196 4.2 3.1 1.0 ND1 A:HIS168 4.2 4.4 1.0 CD2 A:HIS196 4.2 2.9 1.0 CB A:ASP170 4.3 13.2 0.7 CB A:HIS172 4.4 17.1 1.0 CE2 A:PHE185 4.7 10.9 1.0 CZ A:PHE185 4.7 11.7 1.0 CZ A:PHE174 4.7 2.0 1.0 CE1 A:PHE174 4.8 2.0 1.0 C A:HIS172 4.9 14.3 1.0 CA A:HIS196 5.0 2.9 1.0 O A:HOH45 5.0 8.6 1.0

A.Mordini, M.Mori, A.Massaro, V.Calderone, M.Fragai, C.Luchinat. Contribution of Ligand Free Energy of Solvation to Design New Potent Mmps Inhibitors. J.Med.Chem. 2012.
ISSN: ISSN 0022-2623