Fluorine in PDB 3zs0: Human Myeloperoxidase Inactivated By TX2

All present enzymatic activity of Human Myeloperoxidase Inactivated By TX2:
1.11.2.2;

The structure of Human Myeloperoxidase Inactivated By TX2, PDB code: 3zs0 was solved by A.K.Tiden, T.Sjogren, M.Svensson, A.Bernlind, R.Senthilmohan, F.Auchere, H.Norman, P.O.Markgren, S.Gustavsson, S.Schmidt, S.Lundquist, L.V.Forbes, N.J.Magon, G.N.Jameson, H.Eriksson, A.J.Kettle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.905, 64.111, 111.452, 90.00, 97.12, 90.00
R / Rfree (%)	17 / 20.7

The structure of Human Myeloperoxidase Inactivated By TX2 also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Calcium	(Ca)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Fluorine atom in the Human Myeloperoxidase Inactivated By TX2 (pdb code 3zs0). 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 Myeloperoxidase Inactivated By TX2, PDB code: 3zs0:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Myeloperoxidase Inactivated By TX2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Myeloperoxidase Inactivated By TX2 within 5.0Å range: probe atom residue distance (Å) B Occ C:F1579 b:29.2 occ:1.00 F19 C:ZS01579 0.0 29.2 1.0 C16 C:ZS01579 1.3 30.3 1.0 C15 C:ZS01579 2.4 30.6 1.0 C17 C:ZS01579 2.4 29.8 1.0 CE C:MET411 3.0 24.3 1.0 CB C:PRO145 3.6 13.3 1.0 C14 C:ZS01579 3.6 30.4 1.0 C18 C:ZS01579 3.6 30.0 1.0 O C:PRO145 3.9 12.3 1.0 CD1 C:LEU415 4.0 11.4 1.0 SD C:MET411 4.1 27.7 1.0 C C:PRO145 4.1 12.7 1.0 C13 C:ZS01579 4.1 31.2 1.0 CG C:GLU116 4.3 28.1 1.0 CD2 C:LEU415 4.3 11.3 1.0 CA C:PRO145 4.5 13.0 1.0 O A:HOH2099 4.5 13.0 1.0 CG C:PRO145 4.5 14.0 1.0 OE2 C:GLU116 4.5 32.8 1.0 N C:PHE146 4.6 12.1 1.0 CE1 C:PHE147 4.6 15.7 1.0 CD1 C:PHE147 4.7 15.0 1.0 CG C:LEU415 4.8 12.6 1.0 CD C:GLU116 4.8 31.4 1.0 CA C:PHE146 5.0 11.9 1.0

Fluorine binding site 2 out of 2 in the Human Myeloperoxidase Inactivated By TX2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Myeloperoxidase Inactivated By TX2 within 5.0Å range: probe atom residue distance (Å) B Occ D:F1579 b:46.6 occ:1.00 F19 D:ZS01579 0.0 46.6 1.0 C16 D:ZS01579 1.3 45.9 1.0 C15 D:ZS01579 2.4 45.8 1.0 C17 D:ZS01579 2.4 45.5 1.0 O D:HOH2005 3.0 36.5 1.0 O D:PRO145 3.4 20.9 1.0 CB D:PRO145 3.6 21.8 1.0 C18 D:ZS01579 3.6 45.1 1.0 C14 D:ZS01579 3.6 45.6 1.0 CE D:MET411 3.8 38.0 1.0 C D:PRO145 3.9 20.6 1.0 CD2 D:LEU415 4.0 22.6 1.0 C13 D:ZS01579 4.1 45.6 1.0 CD1 D:LEU415 4.2 21.7 1.0 CA D:PRO145 4.4 21.5 1.0 CG D:PRO145 4.4 22.2 1.0 SD D:MET411 4.5 40.1 1.0 N D:PHE146 4.6 19.9 1.0 CE1 D:PHE147 4.7 25.2 1.0 OE1 D:GLU116 4.7 44.1 1.0 CD D:PRO145 4.7 21.8 1.0 CD1 D:PHE147 4.8 23.9 1.0 CG D:LEU415 4.8 22.3 1.0 O B:HOH2087 4.8 25.1 1.0 CA D:PHE146 4.9 19.6 1.0 N D:PRO145 5.0 22.1 1.0

A.K.Tiden, T.Sjogren, M.Svensson, A.Bernlind, R.Senthilmohan, F.Auchere, H.Norman, P.O.Markgren, S.Gustavsson, S.Schmidt, S.Lundquist, L.V.Forbes, N.J.Magon, L.N.Paton, G.N.Jameson, H.Eriksson, A.J.Kettle. 2-Thioxanthines Are Mechanism-Based Inactivators of Myeloperoxidase That Block Oxidative Stress During Inflammation. J.Biol.Chem. V. 286 37578 2011.
ISSN: ISSN 0021-9258
PubMed: 21880720
DOI: 10.1074/JBC.M111.266981