Calcium in PDB 1zp5: Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor

All present enzymatic activity of Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor:
3.4.24.34;

The structure of Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor, PDB code: 1zp5 was solved by C.Campestre, M.Agamennone, P.Tortorella, S.Preziuso, A.Biasone, E.Gavuzzo, G.Pochetti, F.Mazza, H.Tschesche, C.Gallina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.387, 52.675, 67.331, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 25.1

The structure of Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor (pdb code 1zp5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor, PDB code: 1zp5:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca996 b:22.6 occ:1.00 O A:ASP137 2.5 19.5 1.0 O A:GLY171 2.5 23.6 1.0 OD1 A:ASP173 2.5 16.2 1.0 O A:GLY169 2.7 35.1 1.0 O A:HOH1098 2.7 29.7 1.0 O A:HOH1093 3.2 34.7 1.0 CG A:ASP173 3.3 15.2 1.0 C A:ASP137 3.6 19.3 1.0 C A:GLY171 3.6 22.3 1.0 C A:GLY169 3.6 33.4 1.0 OD2 A:ASP173 3.8 14.3 1.0 C A:ILE170 3.9 24.8 1.0 N A:ASP173 4.0 14.4 1.0 O A:ILE170 4.0 23.6 1.0 N A:GLY171 4.1 23.4 1.0 O A:ALA136 4.2 20.6 1.0 ND2 A:ASN139 4.3 24.1 1.0 CA A:ILE170 4.4 27.8 1.0 N A:ILE170 4.4 30.1 1.0 CA A:ASP137 4.4 21.1 1.0 CB A:ASP173 4.4 13.1 1.0 N A:ILE138 4.4 17.5 1.0 CA A:GLY171 4.4 22.8 1.0 CA A:ILE138 4.5 14.7 1.0 C A:GLY172 4.5 15.9 1.0 N A:GLY172 4.5 21.4 1.0 CA A:GLY169 4.5 33.5 1.0 N A:GLY169 4.6 33.6 1.0 CA A:ASP173 4.6 13.7 1.0 CA A:GLY172 4.6 17.0 1.0 O A:GLY167 4.6 30.7 1.0 N A:ASN139 4.6 16.9 1.0 CH2 A:TRP88 4.8 24.1 1.0 C A:GLN168 4.8 34.4 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Complex Between Mmp-8 and A N-Hydroxyurea Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca997 b:15.7 occ:1.00 O A:ASN157 2.4 19.1 1.0 OD2 A:ASP177 2.4 11.9 1.0 O A:GLY155 2.4 16.6 1.0 OE2 A:GLU180 2.4 15.9 1.0 O A:ILE159 2.4 15.7 1.0 OD1 A:ASP154 2.5 14.4 1.0 CG A:ASP177 3.4 10.5 1.0 C A:ILE159 3.4 15.3 1.0 C A:ASN157 3.5 19.9 1.0 CG A:ASP154 3.6 16.6 1.0 C A:GLY155 3.6 17.6 1.0 CD A:GLU180 3.6 16.3 1.0 N A:ILE159 3.7 16.9 1.0 N A:ASN157 3.9 18.8 1.0 CB A:ASP177 3.9 10.9 1.0 C A:PRO156 4.0 18.6 1.0 N A:GLY155 4.1 17.3 1.0 CA A:ILE159 4.1 17.1 1.0 OD2 A:ASP154 4.1 15.2 1.0 C A:ASP154 4.1 17.7 1.0 N A:ASP154 4.1 16.8 1.0 CA A:ASN157 4.2 19.4 1.0 C A:GLY158 4.3 18.7 1.0 OE1 A:GLU180 4.3 15.0 1.0 O A:PRO156 4.3 19.9 1.0 OD1 A:ASP177 4.3 11.3 1.0 N A:LEU160 4.4 13.5 1.0 CB A:ILE159 4.4 17.2 1.0 CA A:GLY155 4.4 16.5 1.0 CA A:ASP154 4.5 16.9 1.0 N A:PRO156 4.5 16.6 1.0 N A:GLY158 4.5 18.7 1.0 O A:ASP154 4.5 18.7 1.0 CA A:PRO156 4.5 18.7 1.0 CG A:GLU180 4.6 15.5 1.0 CB A:ASP154 4.6 16.4 1.0 CA A:LEU160 4.6 14.0 1.0 CA A:GLY158 4.6 19.2 1.0 O A:GLY158 4.9 19.3 1.0

C.Campestre, M.Agamennone, P.Tortorella, S.Preziuso, A.Biasone, E.Gavuzzo, G.Pochetti, F.Mazza, O.Hiller, H.Tschesche, V.Consalvi, C.Gallina. N-Hydroxyurea As Zinc Binding Group in Matrix Metalloproteinase Inhibition: Mode of Binding in A Complex with Mmp-8. Bioorg.Med.Chem.Lett. V. 16 20 2006.
ISSN: ISSN 0960-894X
PubMed: 16242329
DOI: 10.1016/J.BMCL.2005.09.057