Zinc in PDB 3f18: Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide, PDB code: 3f18 was solved by V.Calderone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.16 / 1.13
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.709, 60.326, 53.992, 90.00, 115.07, 90.00
R / Rfree (%)	16.6 / 18.7

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Calcium	(Ca)	3 atoms

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide (pdb code 3f18). 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 Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide, PDB code: 3f18:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide


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 Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn264 b:6.1 occ:1.00 NE2 A:HIS218 2.1 6.5 1.0 NE2 A:HIS228 2.1 6.7 1.0 O3 A:HS50 2.1 11.4 1.0 NE2 A:HIS222 2.1 5.5 1.0 O2 A:HS50 2.2 7.5 1.0 C9 A:HS50 2.8 11.2 1.0 N1 A:HS50 2.9 9.6 1.0 CD2 A:HIS218 3.0 6.4 1.0 CE1 A:HIS228 3.0 7.2 1.0 CE1 A:HIS218 3.1 7.2 1.0 CE1 A:HIS222 3.1 6.2 1.0 CD2 A:HIS228 3.1 7.0 1.0 CD2 A:HIS222 3.1 5.4 1.0 O A:HOH14 4.1 8.8 1.0 ND1 A:HIS228 4.1 7.3 1.0 ND1 A:HIS218 4.2 6.8 1.0 CG A:HIS218 4.2 6.1 1.0 ND1 A:HIS222 4.2 6.1 1.0 CG A:HIS228 4.2 7.2 1.0 OE1 A:GLU219 4.2 8.0 1.0 CG A:HIS222 4.2 5.2 1.0 C10 A:HS50 4.3 13.6 1.0 O A:HOH301 4.6 19.8 1.0 C5 A:HS50 4.8 12.7 1.0 O A:HOH104 4.8 22.6 1.0 CE A:MET236 4.9 7.3 1.0 C3 A:HS50 5.0 13.2 1.0 C7 A:HS50 5.0 12.5 1.0 O A:HOH405 5.0 39.2 1.0 CD A:GLU219 5.0 6.9 1.0 OE2 A:GLU219 5.0 8.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide


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 Catalytic Domain of Human MMP12 Complexed with the Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn265 b:8.2 occ:1.00 NE2 A:HIS183 2.0 10.7 1.0 OD1 A:ASP170 2.0 8.0 0.7 NE2 A:HIS168 2.0 8.9 1.0 ND1 A:HIS196 2.1 6.6 1.0 CE1 A:HIS183 2.7 12.4 1.0 CD2 A:HIS168 2.9 9.2 1.0 CG A:ASP170 2.9 11.2 0.7 CE1 A:HIS196 3.0 7.5 1.0 CE1 A:HIS168 3.0 8.2 1.0 CG A:HIS196 3.1 6.3 1.0 CD2 A:HIS183 3.1 11.7 1.0 OD2 A:ASP170 3.2 9.4 0.7 CB A:HIS196 3.5 6.2 1.0 ND1 A:HIS183 3.9 11.8 1.0 CG A:HIS168 4.1 9.7 1.0 O A:HIS172 4.1 14.1 1.0 ND1 A:HIS168 4.1 8.7 1.0 NE2 A:HIS196 4.1 7.1 1.0 CG A:HIS183 4.1 8.7 1.0 CD2 A:HIS196 4.2 6.5 1.0 CB A:ASP170 4.3 14.3 0.7 CB A:HIS172 4.5 16.4 1.0 CE2 A:PHE185 4.5 13.3 1.0 CZ A:PHE185 4.6 13.1 1.0 CZ A:PHE174 4.6 7.9 1.0 CE1 A:PHE174 4.7 8.1 1.0 C A:HIS172 5.0 14.4 1.0 CA A:HIS196 5.0 5.8 1.0

I.Bertini, V.Calderone, M.Fragai, A.Giachetti, M.Loconte, C.Luchinat, M.Maletta, C.Nativi, K.J.Yeo. Exploring the Subtleties of Drug-Receptor Interactions: the Case of Matrix Metalloproteinases. J.Am.Chem.Soc. V. 129 2466 2007.
ISSN: ISSN 0002-7863
PubMed: 17269766
DOI: 10.1021/JA065156Z