Zinc in PDB 2hu6: Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor

All present enzymatic activity of Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor:
3.4.24.65;

The structure of Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor, PDB code: 2hu6 was solved by C.Mannino, M.Nievo, F.Machetti, A.Papakyriakou, V.Calderone, M.Fragai, A.Guarna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.68 / 1.32
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.250, 60.179, 53.974, 90.00, 114.59, 90.00
R / Rfree (%)	16.1 / 18.2

The structure of Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor (pdb code 2hu6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor, PDB code: 2hu6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn264 b:7.7 occ:1.00 NE2 A:HIS218 2.1 7.4 1.0 NE2 A:HIS228 2.1 8.7 1.0 NE2 A:HIS222 2.1 6.8 1.0 O A:HAE269 2.1 13.4 1.0 O2 A:HAE269 2.4 18.0 1.0 O A:HOH655 2.4 29.3 1.0 N A:HAE269 2.9 12.9 1.0 C2 A:HAE269 3.0 15.8 1.0 CD2 A:HIS218 3.0 6.7 1.0 CE1 A:HIS228 3.0 8.8 1.0 CD2 A:HIS222 3.1 6.8 1.0 CD2 A:HIS228 3.1 8.7 1.0 CE1 A:HIS218 3.1 7.3 1.0 CE1 A:HIS222 3.1 7.3 1.0 O A:HOH416 4.2 11.0 1.0 ND1 A:HIS228 4.2 8.8 1.0 CG A:HIS218 4.2 6.7 1.0 ND1 A:HIS218 4.2 7.0 1.0 CG A:HIS228 4.2 8.3 1.0 CG A:HIS222 4.2 6.4 1.0 ND1 A:HIS222 4.2 7.7 1.0 O A:HOH656 4.3 28.6 1.0 OE1 A:GLU219 4.3 11.1 1.0 C1 A:HAE269 4.4 17.1 1.0 O A:HOH588 4.4 34.2 1.0 C12 A:37A400 4.5 20.0 1.0 O A:HOH594 4.8 29.6 1.0 OE2 A:GLU219 4.8 10.8 1.0 CD A:GLU219 4.9 8.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Mmp-12 in Complex with Acetohydroxamic Acid and A Bicyclic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn265 b:8.1 occ:1.00 OD2 A:ASP170 2.0 10.2 1.0 NE2 A:HIS183 2.0 10.2 1.0 NE2 A:HIS168 2.0 8.4 1.0 ND1 A:HIS196 2.1 8.0 1.0 CE1 A:HIS183 2.9 11.7 1.0 CG A:ASP170 2.9 12.9 1.0 CD2 A:HIS168 2.9 9.1 1.0 CE1 A:HIS196 3.0 9.0 1.0 CE1 A:HIS168 3.1 8.7 1.0 CG A:HIS196 3.1 7.3 1.0 CD2 A:HIS183 3.1 11.0 1.0 OD1 A:ASP170 3.2 11.1 1.0 CB A:HIS196 3.5 6.9 1.0 ND1 A:HIS183 4.1 11.4 1.0 CG A:HIS168 4.1 9.4 1.0 NE2 A:HIS196 4.1 7.5 1.0 ND1 A:HIS168 4.1 8.6 1.0 O A:HIS172 4.2 12.9 1.0 CG A:HIS183 4.2 8.8 1.0 CD2 A:HIS196 4.2 7.4 1.0 CB A:ASP170 4.2 14.0 1.0 CE2 A:PHE185 4.5 15.0 1.0 CZ A:PHE185 4.6 14.8 1.0 CZ A:PHE174 4.6 7.9 1.0 CB A:HIS172 4.7 15.6 1.0 CE1 A:PHE174 4.7 8.3 1.0 CA A:HIS196 5.0 6.6 1.0

C.Mannino, M.Nievo, F.Machetti, A.Papakyriakou, V.Calderone, M.Fragai, A.Guarna. Synthesis of Bicyclic Molecular Scaffolds (Btaa): An Investigation Towards New Selective Mmp-12 Inhibitors. Bioorg.Med.Chem. V. 14 7392 2006.
ISSN: ISSN 0968-0896
PubMed: 16899369
DOI: 10.1016/J.BMC.2006.07.028