Zinc in PDB 4guy: Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide

All present enzymatic activity of Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide:
3.4.24.65;

The structure of Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide, PDB code: 4guy was solved by V.Calderone, M.Fragai, C.Luchinat, A.Massaro, A.Mordini, M.Mori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.56 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	50.989, 61.107, 54.213, 90.00, 114.50, 90.00
R / Rfree (%)	22.7 / 29.3

The structure of Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide (pdb code 4guy). 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 MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide, PDB code: 4guy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:11.1 occ:1.00 NE2 A:HIS222 2.1 9.0 1.0 O2 A:KLJ306 2.1 17.9 1.0 NE2 A:HIS218 2.2 6.3 1.0 NE2 A:HIS228 2.3 12.6 1.0 O4 A:KLJ306 2.4 15.0 1.0 CD2 A:HIS218 2.9 6.6 1.0 CD2 A:HIS222 2.9 9.0 1.0 C10 A:KLJ306 2.9 17.7 1.0 N2 A:KLJ306 3.0 16.8 1.0 CD2 A:HIS228 3.3 11.8 1.0 CE1 A:HIS222 3.3 8.9 1.0 CE1 A:HIS228 3.3 11.6 1.0 CE1 A:HIS218 3.4 6.7 1.0 O A:HOH475 3.7 6.4 1.0 CG A:HIS222 4.1 8.9 1.0 CG A:HIS218 4.2 6.7 1.0 OE1 A:GLU219 4.2 6.0 1.0 ND1 A:HIS222 4.3 8.8 1.0 ND1 A:HIS218 4.3 6.6 1.0 C11 A:KLJ306 4.3 18.1 1.0 ND1 A:HIS228 4.4 11.6 1.0 CG A:HIS228 4.4 11.9 1.0 O A:HOH476 4.7 10.5 1.0 N1 A:KLJ306 4.7 18.1 1.0 C1 A:KLJ306 4.8 15.9 1.0 O A:HOH477 4.9 10.8 1.0

Zinc binding site 2 out of 2 in the Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human MMP12 Catalytic Domain in Complex with*N*-Hydroxy-2-(2-(4- Methoxyphenyl)Ethylsulfonamido)Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:13.5 occ:1.00 NE2 A:HIS168 2.1 15.4 1.0 OD1 A:ASP170 2.1 11.7 0.7 CE1 A:HIS183 2.1 13.2 1.0 ND1 A:HIS196 2.2 9.7 1.0 NE2 A:HIS183 2.6 13.7 1.0 CD2 A:HIS168 2.9 15.4 1.0 CG A:ASP170 3.0 12.7 0.7 CE1 A:HIS196 3.1 9.2 1.0 CG A:HIS196 3.2 9.6 1.0 OD2 A:ASP170 3.2 11.5 0.7 CE1 A:HIS168 3.2 15.6 1.0 ND1 A:HIS183 3.4 12.9 1.0 CB A:HIS196 3.5 9.6 1.0 CD2 A:HIS183 3.9 13.2 1.0 CG A:HIS168 4.1 15.1 1.0 ND1 A:HIS168 4.2 15.3 1.0 O A:HIS172 4.3 18.8 1.0 CG A:HIS183 4.3 12.2 1.0 NE2 A:HIS196 4.3 9.3 1.0 CD2 A:HIS196 4.3 9.7 1.0 CB A:ASP170 4.4 13.8 0.7 CE2 A:PHE185 4.6 16.8 1.0 CZ A:PHE174 4.6 11.1 1.0 CB A:HIS172 4.6 24.4 1.0 CE1 A:PHE174 4.7 11.5 1.0 O A:HOH406 4.8 9.1 1.0 CZ A:PHE185 4.9 16.9 1.0 C A:HIS172 4.9 21.2 1.0 CA A:HIS196 5.0 9.8 1.0

M.Mori, A.Massaro, V.Calderone, M.Fragai, C.Luchinat, A.Mordini. Contribution of Free Energy of Solvation to Ligand Affinity in New Potent Mmps Inhibitors. To Be Published.