Zinc in PDB 9csx: Matrix Metalloproteinase-10 Proenzyme

All present enzymatic activity of Matrix Metalloproteinase-10 Proenzyme:
3.4.24.22;

The structure of Matrix Metalloproteinase-10 Proenzyme, PDB code: 9csx was solved by E.A.Isiorho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.12 / 1.67
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.841, 72.003, 54.495, 90, 130.82, 90
R / Rfree (%)	18.9 / 21.3

The structure of Matrix Metalloproteinase-10 Proenzyme also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Matrix Metalloproteinase-10 Proenzyme (pdb code 9csx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Matrix Metalloproteinase-10 Proenzyme, PDB code: 9csx:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Matrix Metalloproteinase-10 Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Matrix Metalloproteinase-10 Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn308 b:14.1 occ:1.00 OD2 A:ASP169 2.0 11.9 1.0 NE2 A:HIS167 2.2 14.6 1.0 ND1 A:HIS195 2.2 14.9 1.0 NE2 A:HIS182 2.2 13.2 1.0 CG A:ASP169 2.9 14.7 1.0 CD2 A:HIS167 3.0 15.9 1.0 HH A:TYR184 3.0 18.6 1.0 HD2 A:HIS167 3.0 19.1 1.0 HB2 A:HIS195 3.1 25.0 1.0 CE1 A:HIS182 3.1 18.1 1.0 OD1 A:ASP169 3.1 15.4 1.0 CE1 A:HIS195 3.1 14.4 1.0 CG A:HIS195 3.2 14.9 1.0 HE1 A:HIS182 3.2 21.8 1.0 CD2 A:HIS182 3.2 14.8 1.0 HE1 A:HIS195 3.3 17.3 1.0 CE1 A:HIS167 3.3 17.2 1.0 HD2 A:HIS182 3.4 17.8 1.0 CB A:HIS195 3.5 20.8 1.0 HB3 A:HIS195 3.6 25.0 1.0 HE1 A:HIS167 3.6 20.7 1.0 OH A:TYR184 3.7 15.5 1.0 O A:TYR171 4.1 15.4 1.0 HE2 A:TYR184 4.1 17.7 1.0 CG A:HIS167 4.2 13.3 1.0 ND1 A:HIS182 4.2 12.7 1.0 NE2 A:HIS195 4.3 14.1 1.0 CB A:ASP169 4.3 13.8 1.0 ND1 A:HIS167 4.3 13.2 1.0 CD2 A:HIS195 4.3 12.8 1.0 CG A:HIS182 4.3 14.0 1.0 HB2 A:TYR171 4.4 18.9 1.0 HB3 A:ASP169 4.4 16.6 1.0 HE2 A:PHE173 4.4 13.2 1.0 CE2 A:PHE173 4.6 11.0 1.0 HZ A:PHE173 4.6 13.7 1.0 CZ A:TYR184 4.7 13.5 1.0 HB2 A:ASP169 4.7 16.6 1.0 O A:HOH498 4.7 28.2 1.0 CE2 A:TYR184 4.7 14.7 1.0 H A:TYR171 4.7 18.1 1.0 CZ A:PHE173 4.7 11.4 1.0 CA A:HIS195 5.0 10.6 1.0

Zinc binding site 2 out of 4 in the Matrix Metalloproteinase-10 Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Matrix Metalloproteinase-10 Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn309 b:12.9 occ:1.00 NE2 A:HIS221 2.0 15.2 1.0 NE2 A:HIS227 2.0 10.7 1.0 NE2 A:HIS217 2.0 13.2 1.0 SG A:CYS91 2.3 13.0 1.0 CD2 A:HIS227 2.9 13.1 1.0 HB3 A:CYS91 2.9 16.3 1.0 CE1 A:HIS221 3.0 17.6 1.0 CB A:CYS91 3.0 13.6 1.0 CD2 A:HIS217 3.0 11.9 1.0 HD2 A:HIS227 3.0 15.7 1.0 CD2 A:HIS221 3.0 14.6 1.0 CE1 A:HIS217 3.0 10.6 1.0 CE1 A:HIS227 3.1 10.3 1.0 HB2 A:CYS91 3.1 16.3 1.0 HE1 A:HIS221 3.1 21.2 1.0 HD2 A:HIS217 3.2 14.3 1.0 HD2 A:HIS221 3.2 17.5 1.0 HB A:VAL93 3.2 16.9 1.0 HE1 A:HIS217 3.2 12.7 1.0 HE1 A:HIS227 3.3 12.4 1.0 HG21 A:VAL93 4.1 15.2 1.0 CG A:HIS227 4.1 14.1 1.0 HG23 A:VAL93 4.1 15.2 1.0 ND1 A:HIS221 4.1 19.4 1.0 CB A:VAL93 4.1 14.1 1.0 H A:VAL93 4.1 16.6 1.0 ND1 A:HIS217 4.1 12.4 1.0 ND1 A:HIS227 4.1 10.4 1.0 CG A:HIS221 4.1 14.9 1.0 CG A:HIS217 4.1 12.6 1.0 HE3 A:MET235 4.2 19.5 1.0 HE1 A:MET235 4.2 19.5 1.0 HA A:PRO237 4.3 18.7 1.0 OE2 A:GLU218 4.3 15.9 1.0 CG2 A:VAL93 4.3 12.6 1.0 OE1 A:GLU218 4.4 11.8 1.0 CA A:CYS91 4.5 14.3 1.0 CD A:GLU218 4.7 13.1 1.0 CE A:MET235 4.7 16.2 1.0 HB3 A:PRO237 4.8 16.9 1.0 HG11 A:VAL93 4.8 20.1 1.0 N A:VAL93 4.8 13.8 1.0 HA A:CYS91 4.8 17.2 1.0 HD1 A:HIS221 4.9 23.3 1.0 HD1 A:HIS217 4.9 14.9 1.0 HA A:GLU218 4.9 15.8 1.0 HD1 A:HIS227 4.9 12.4 1.0 C A:CYS91 5.0 17.1 1.0 CG1 A:VAL93 5.0 16.7 1.0

Zinc binding site 3 out of 4 in the Matrix Metalloproteinase-10 Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Matrix Metalloproteinase-10 Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn310 b:17.6 occ:1.00 H2 A:IMD301 1.9 19.0 1.0 HN1 A:IMD301 1.9 18.5 1.0 OE1 A:GLU155 2.1 18.8 1.0 C2 A:IMD301 2.3 15.8 1.0 N1 A:IMD301 2.3 15.4 1.0 CD A:GLU155 2.9 13.3 1.0 OE2 A:GLU155 3.0 16.2 1.0 N3 A:IMD301 3.7 22.8 1.0 C5 A:IMD301 3.7 10.1 1.0 HA2 A:GLY189 3.9 20.3 1.0 HN3 A:IMD301 4.3 27.4 1.0 C4 A:IMD301 4.3 19.7 1.0 CG A:GLU155 4.3 23.0 1.0 H5 A:IMD301 4.3 12.1 1.0 HB2 A:GLU155 4.4 22.5 1.0 HE2 A:MET159 4.5 25.6 1.0 HG2 A:GLU155 4.6 27.7 1.0 CA A:GLY189 4.8 16.9 1.0 HG3 A:GLU155 4.9 27.7 1.0 CB A:GLU155 4.9 18.8 1.0 HA A:GLU155 5.0 20.8 1.0

Zinc binding site 4 out of 4 in the Matrix Metalloproteinase-10 Proenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Matrix Metalloproteinase-10 Proenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn311 b:33.3 occ:1.00 HN1 A:IMD302 2.0 25.2 1.0 OE2 A:GLU84 2.1 23.7 1.0 H2 A:IMD302 2.2 31.9 1.0 N1 A:IMD302 2.5 21.0 1.0 C2 A:IMD302 2.6 26.6 1.0 CD A:GLU84 2.8 28.5 1.0 OE1 A:GLU84 2.9 26.3 1.0 C5 A:IMD302 3.8 31.1 1.0 N3 A:IMD302 3.9 23.2 1.0 CG A:GLU84 4.3 22.4 1.0 H5 A:IMD302 4.4 37.3 1.0 C4 A:IMD302 4.5 30.2 1.0 HG2 A:GLU84 4.5 26.9 1.0 HG3 A:GLU84 4.6 26.9 1.0 HN3 A:IMD302 4.6 27.9 1.0

E.A.Isiorho, E.A.Isiorho. N/A N/A.