Fluorine 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:

Calcium	(Ca)	3 atoms
Zinc	(Zn)	2 atoms

The binding sites of Fluorine 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 Fluorine atom.
In total only one binding site of Fluorine was 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:

Fluorine binding site 1 out of 1 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 Fluorine with other atoms in the F 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:F0 b:13.3 occ:1.00 F1 A:HS50 0.0 13.3 1.0 C4 A:HS50 1.3 12.8 1.0 C2 A:HS50 2.4 13.3 1.0 C7 A:HS50 2.4 12.5 1.0 CB A:HIS218 3.0 5.7 1.0 CG A:HIS218 3.0 6.1 1.0 ND1 A:HIS218 3.3 6.8 1.0 C1 A:HS50 3.6 13.3 1.0 C5 A:HS50 3.7 12.7 1.0 CD2 A:HIS218 3.7 6.4 1.0 O A:HOH326 3.8 24.9 1.0 CE1 A:HIS218 4.0 7.2 1.0 O A:HOH345 4.0 19.7 1.0 C3 A:HS50 4.2 13.2 1.0 CA A:THR215 4.2 5.5 1.0 NE2 A:HIS218 4.2 6.5 1.0 O A:LEU214 4.3 6.2 1.0 O A:VAL235 4.4 9.2 1.0 O A:THR215 4.4 5.7 1.0 CA A:HIS218 4.5 5.6 1.0 CD1 A:TYR240 4.6 14.4 1.0 CB A:TYR240 4.8 14.8 1.0 CG2 A:THR215 4.8 6.5 1.0 C A:THR215 4.8 5.5 1.0 CA A:TYR240 4.8 15.1 1.0 N A:THR215 4.9 5.5 1.0 C A:LEU214 4.9 6.0 1.0 CB A:THR215 4.9 5.7 1.0 O A:PHE237 5.0 12.3 1.0 OG1 A:THR215 5.0 6.2 1.0 N A:HIS218 5.0 5.4 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