Calcium in PDB 1jh1: Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor

All present enzymatic activity of Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor:
3.4.24.34;

The structure of Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor, PDB code: 1jh1 was solved by J.Schroder, A.Henke, H.Wenzel, H.Brandstetter, H.G.Stammler, A.Stammler, W.D.Pfeiffer, H.Tschesche, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.990, 69.380, 72.090, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 26.4

The structure of Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Zinc	(Zn)	2 atoms

The binding sites of Calcium atom in the Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor (pdb code 1jh1). 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 Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor, PDB code: 1jh1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived 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 Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca996 b:3.8 occ:1.00 O A:GLY171 2.6 11.9 1.0 O A:GLY169 2.6 14.7 1.0 O A:HOH22 2.7 15.7 1.0 O A:ASP137 2.7 12.6 1.0 OD1 A:ASP173 3.1 13.8 1.0 C A:GLY169 3.3 14.3 1.0 OD2 A:ASP173 3.4 13.2 1.0 CG A:ASP173 3.5 11.9 1.0 C A:GLY171 3.5 10.4 1.0 C A:ILE170 3.7 12.6 1.0 C A:ASP137 3.8 11.7 1.0 O A:ILE170 3.9 12.4 1.0 N A:GLY171 3.9 11.4 1.0 N A:ILE170 4.0 14.4 1.0 N A:ASP173 4.1 7.3 1.0 CA A:GLY169 4.1 15.6 1.0 CA A:ILE170 4.1 12.3 1.0 N A:GLY169 4.1 16.4 1.0 CA A:GLY171 4.3 11.4 1.0 C A:GLN168 4.3 17.5 1.0 O A:GLY167 4.3 13.7 1.0 N A:GLY172 4.4 9.4 1.0 O A:GLN168 4.4 17.2 1.0 CA A:ASP137 4.5 12.2 1.0 CA A:GLY172 4.5 8.9 1.0 O A:ALA136 4.6 15.7 1.0 C A:GLY172 4.6 7.2 1.0 CB A:ASP173 4.7 9.6 1.0 CH2 A:TRP88 4.8 12.5 1.0 ND2 A:ASN139 4.8 14.1 1.0 CA A:ASP173 4.8 7.7 1.0 N A:ILE138 4.9 10.3 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived 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 Mmp-8 Complexed with A 6H-1,3,4- Thiadiazine Derived Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca997 b:2.4 occ:1.00 O A:GLY155 2.5 9.2 1.0 O A:ASN157 2.6 13.0 1.0 OE2 A:GLU180 2.6 14.8 1.0 OD2 A:ASP177 2.7 10.4 1.0 O A:ILE159 2.8 8.1 1.0 OD1 A:ASP154 2.8 7.6 1.0 C A:ILE159 3.4 4.7 1.0 CG A:ASP177 3.4 11.4 1.0 CG A:ASP154 3.5 6.5 1.0 N A:ILE159 3.6 6.4 1.0 C A:GLY155 3.6 9.9 1.0 C A:ASN157 3.7 10.5 1.0 CD A:GLU180 3.8 10.7 1.0 OD2 A:ASP154 3.9 5.9 1.0 CA A:ILE159 3.9 4.8 1.0 N A:GLY155 3.9 8.8 1.0 CB A:ASP177 4.0 9.4 1.0 OD1 A:ASP177 4.1 11.7 1.0 C A:ASP154 4.1 7.8 1.0 N A:ASP154 4.2 5.5 1.0 N A:LEU160 4.2 4.1 1.0 C A:GLY158 4.2 6.0 1.0 N A:ASN157 4.2 10.5 1.0 C A:PRO156 4.3 10.7 1.0 CB A:ILE159 4.4 3.9 1.0 CA A:GLY155 4.4 8.8 1.0 CA A:ASP154 4.4 6.2 1.0 CG A:GLU180 4.5 10.6 1.0 CA A:ASN157 4.5 10.8 1.0 O A:PRO156 4.5 11.2 1.0 CA A:LEU160 4.5 3.2 1.0 N A:GLY158 4.5 9.2 1.0 CA A:GLY158 4.6 8.1 1.0 CB A:ASP154 4.6 6.0 1.0 N A:PRO156 4.6 10.0 1.0 O A:ASP154 4.6 9.3 1.0 CA A:PRO156 4.7 10.2 1.0 OE1 A:GLU180 4.8 12.9 1.0 O A:GLY158 4.9 6.8 1.0

J.Schroder, A.Henke, H.Wenzel, H.Brandstetter, H.G.Stammler, A.Stammler, W.D.Pfeiffer, H.Tschesche. Structure-Based Design and Synthesis of Potent Matrix Metalloproteinase Inhibitors Derived From A 6H-1,3,4-Thiadiazine Scaffold. J.Med.Chem. V. 44 3231 2001.
ISSN: ISSN 0022-2623
PubMed: 11563922
DOI: 10.1021/JM010887P