Fluorine in PDB 2vz2: Human Mao B in Complex with Mofegiline

All present enzymatic activity of Human Mao B in Complex with Mofegiline:
1.4.3.4;

The structure of Human Mao B in Complex with Mofegiline, PDB code: 2vz2 was solved by D.Bonivento, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.74 / 2.30
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	132.026, 223.730, 86.629, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 22.9

The binding sites of Fluorine atom in the Human Mao B in Complex with Mofegiline (pdb code 2vz2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Mao B in Complex with Mofegiline, PDB code: 2vz2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Mao B in Complex with Mofegiline


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Mao B in Complex with Mofegiline within 5.0Å range: probe atom residue distance (Å) B Occ A:F1503 b:31.9 occ:1.00 F1 A:MFG1503 0.0 31.9 1.0 C2 A:MFG1503 1.3 31.2 1.0 C14 A:MFG1503 2.4 31.1 1.0 C3 A:MFG1503 2.4 30.3 1.0 CA A:ILE199 3.3 20.6 1.0 O A:ILE198 3.5 19.8 1.0 C13 A:MFG1503 3.6 31.0 1.0 C4 A:MFG1503 3.6 30.5 1.0 CD2 A:LEU171 3.7 19.0 1.0 CG2 A:ILE199 3.8 22.0 1.0 CB A:ILE199 3.8 20.9 1.0 NE2 A:GLN206 3.8 16.8 1.0 O A:ILE199 4.0 20.8 1.0 C A:ILE199 4.1 20.4 1.0 CG A:LEU171 4.1 19.5 1.0 C A:ILE198 4.1 19.6 1.0 N A:ILE199 4.1 20.0 1.0 C5 A:MFG1503 4.1 30.9 1.0 CD A:GLN206 4.6 18.5 1.0 SG A:CYS172 4.7 23.2 1.0 O A:HOH2127 4.7 13.2 1.0

Fluorine binding site 2 out of 2 in the Human Mao B in Complex with Mofegiline


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Mao B in Complex with Mofegiline within 5.0Å range: probe atom residue distance (Å) B Occ B:F1498 b:34.7 occ:1.00 F1 B:MFG1498 0.0 34.7 1.0 C2 B:MFG1498 1.3 33.4 1.0 C14 B:MFG1498 2.4 32.6 1.0 C3 B:MFG1498 2.4 32.6 1.0 CA B:ILE199 3.3 20.5 1.0 O B:ILE198 3.5 20.1 1.0 CD2 B:LEU171 3.6 18.8 1.0 C13 B:MFG1498 3.6 32.3 1.0 C4 B:MFG1498 3.6 33.0 1.0 NE2 B:GLN206 3.9 15.6 1.0 O B:ILE199 3.9 20.5 1.0 CB B:ILE199 3.9 20.6 1.0 CG2 B:ILE199 4.0 21.7 1.0 C B:ILE199 4.0 20.4 1.0 N B:ILE199 4.1 20.1 1.0 C B:ILE198 4.1 19.9 1.0 C5 B:MFG1498 4.1 32.8 1.0 CG B:LEU171 4.2 19.5 1.0 O B:HOH2101 4.5 11.6 1.0 CD B:GLN206 4.6 18.8 1.0 SG B:CYS172 4.8 22.4 1.0 OH B:TYR326 5.0 22.2 1.0

E.M.Milczek, D.Bonivento, C.Binda, A.Mattevi, I.A.Mcdonald, D.E.Edmondson. Structural and Mechanistic Studies of Mofegiline Inhibition of Recombinant Human Monoamine Oxidase B. J. Med. Chem. V. 51 8019 2008.
ISSN: ISSN 1520-4804
PubMed: 19053775
DOI: 10.1021/JM8011867