Zinc in PDB 5h8x: Crystal Structure of the Complex Mmp-8/BF471 (Catechol Inhibitor)

All present enzymatic activity of Crystal Structure of the Complex Mmp-8/BF471 (Catechol Inhibitor):
3.4.24.34;

The structure of Crystal Structure of the Complex Mmp-8/BF471 (Catechol Inhibitor), PDB code: 5h8x was solved by G.Pochetti, R.Montanari, D.Capelli, P.Tortorella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.67 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.910, 68.460, 68.530, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 21.7

The structure of Crystal Structure of the Complex Mmp-8/BF471 (Catechol Inhibitor) also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of the Complex Mmp-8/BF471 (Catechol Inhibitor) (pdb code 5h8x). 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 the Complex Mmp-8/BF471 (Catechol Inhibitor), PDB code: 5h8x:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Complex Mmp-8/BF471 (Catechol 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 the Complex Mmp-8/BF471 (Catechol Inhibitor) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:9.0 occ:1.00 OD2 A:ASP149 2.0 10.6 1.0 NE2 A:HIS162 2.0 8.7 1.0 NE2 A:HIS147 2.0 7.1 1.0 ND1 A:HIS175 2.1 8.7 1.0 CE1 A:HIS162 2.9 9.6 1.0 CG A:ASP149 2.9 11.2 1.0 CD2 A:HIS147 2.9 7.8 1.0 CE1 A:HIS175 3.0 8.4 1.0 CE1 A:HIS147 3.1 6.7 1.0 CD2 A:HIS162 3.1 7.9 1.0 CG A:HIS175 3.1 7.4 1.0 OD1 A:ASP149 3.2 11.2 1.0 CB A:HIS175 3.5 7.9 1.0 ND1 A:HIS162 4.1 8.9 1.0 CG A:HIS147 4.1 7.0 1.0 ND1 A:HIS147 4.1 8.1 1.0 NE2 A:HIS175 4.1 8.5 1.0 CG A:HIS162 4.2 7.9 1.0 CD2 A:HIS175 4.2 8.3 1.0 CB A:ASP149 4.2 12.3 1.0 CE2 A:PHE164 4.3 14.1 1.0 O A:SER151 4.3 11.7 1.0 CZ A:PHE164 4.6 18.0 1.0 CZ A:PHE153 4.6 7.8 1.0 O A:HOH478 4.8 13.8 1.0 CE2 A:PHE153 4.8 8.3 1.0 CA A:HIS175 4.9 6.6 1.0 O A:HOH479 5.0 10.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Complex Mmp-8/BF471 (Catechol 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 the Complex Mmp-8/BF471 (Catechol Inhibitor) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn304 b:9.8 occ:1.00 OAD A:7FY306 1.8 19.2 0.2 NE2 A:HIS207 2.0 10.2 1.0 NE2 A:HIS197 2.1 9.8 1.0 NE2 A:HIS201 2.1 8.8 1.0 CAW A:7FY306 2.5 19.4 0.2 CAE A:5XT305 2.6 17.9 0.8 CAG A:7FY306 2.7 20.9 0.2 CAF A:5XT305 2.8 18.8 0.8 CD2 A:HIS207 2.9 12.2 1.0 CE1 A:HIS207 3.0 12.3 1.0 CE1 A:HIS197 3.0 10.1 1.0 CD2 A:HIS201 3.0 8.8 1.0 CD2 A:HIS197 3.1 7.3 1.0 CE1 A:HIS201 3.1 10.2 1.0 CAR A:5XT305 3.5 18.1 0.8 CAR A:7FY306 3.8 18.6 0.2 CAS A:5XT305 3.8 23.1 0.8 CAS A:7FY306 4.0 22.6 0.2 CG A:HIS207 4.1 11.9 1.0 ND1 A:HIS207 4.1 11.5 1.0 OAA A:5XT305 4.1 16.0 0.8 ND1 A:HIS197 4.1 9.7 1.0 ND1 A:HIS201 4.2 9.6 1.0 CG A:HIS197 4.2 6.9 1.0 CG A:HIS201 4.2 9.3 1.0 CAW A:5XT305 4.3 18.4 0.8 OAA A:7FY306 4.4 17.6 0.2 CAG A:5XT305 4.4 23.2 0.8 O A:HOH458 4.6 22.7 1.0 CE A:MET215 4.7 10.9 1.0 OE1 A:GLU198 4.7 10.0 1.0 OE2 A:GLU198 4.7 11.2 1.0 NAQ A:5XT305 4.7 25.2 0.8 NAQ A:7FY306 4.8 24.1 0.2 CAE A:7FY306 4.8 19.8 0.2 CAF A:7FY306 4.9 21.3 0.2

M.Tauro, A.Laghezza, F.Loiodice, L.Piemontese, A.Caradonna, D.Capelli, R.Montanari, G.Pochetti, A.Di Pizio, M.Agamennone, C.Campestre, P.Tortorella. Catechol-Based Matrix Metalloproteinase Inhibitors with Additional Antioxidative Activity. J Enzyme Inhib Med Chem V. 31 25 2016.
ISSN: ESSN 1475-6374
PubMed: 27556138
DOI: 10.1080/14756366.2016.1217853