Fluorine in PDB 6il0: K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae

All present enzymatic activity of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae:
3.5.1.88;

The structure of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae, PDB code: 6il0 was solved by I.H.Lee, L.W.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.91 / 1.93
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	58.682, 58.682, 265.531, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 23.1

The structure of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae also contains other interesting chemical elements:

Nickel

(Ni)

3 atoms

The binding sites of Fluorine atom in the K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae (pdb code 6il0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae, PDB code: 6il0:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:43.2 occ:1.00 F1 A:K3U201 0.0 43.2 1.0 C12 A:K3U201 1.3 46.2 1.0 NI A:NI202 2.1 23.8 1.0 F2 A:K3U201 2.2 76.7 1.0 F A:K3U201 2.2 23.4 1.0 C11 A:K3U201 2.3 47.8 1.0 N A:LEU100 2.9 29.5 1.0 OD1 A:CSD99 3.0 32.1 1.0 CA A:CSD99 3.1 28.7 1.0 NE2 A:GLN51 3.1 22.2 1.0 C3 A:K3U201 3.1 49.5 1.0 SG A:CSD99 3.1 32.7 1.0 C A:CSD99 3.4 28.4 1.0 NE2 A:HIS141 3.5 22.9 1.0 CB A:CSD99 3.5 32.3 1.0 CD A:GLN51 3.9 23.3 1.0 NE2 A:HIS145 4.0 19.8 1.0 OE1 A:GLN51 4.0 23.4 1.0 CA A:LEU100 4.0 28.6 1.0 C2 A:K3U201 4.1 53.9 1.0 CB A:LEU100 4.1 29.3 1.0 O A:GLY98 4.2 29.8 1.0 CG A:LEU100 4.2 30.8 1.0 C4 A:K3U201 4.2 44.5 1.0 N A:CSD99 4.2 23.9 1.0 CE1 A:HIS141 4.3 26.5 1.0 CD2 A:HIS141 4.4 25.6 1.0 N A:SER101 4.4 24.8 1.0 OD2 A:CSD99 4.6 35.6 1.0 OE2 A:GLU142 4.6 27.2 1.0 O A:CSD99 4.6 28.2 1.0 C A:GLY98 4.7 27.5 1.0 CD1 A:LEU100 4.7 33.5 1.0 S A:K3U201 4.7 64.6 1.0 C A:LEU100 4.8 26.3 1.0 CE1 A:HIS145 4.8 25.4 1.0 CD2 A:HIS145 4.9 18.6 1.0 O A:GLY46 4.9 24.7 1.0 O1 A:K3U201 5.0 39.0 1.0

Fluorine binding site 2 out of 3 in the K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:23.4 occ:1.00 F A:K3U201 0.0 23.4 1.0 C12 A:K3U201 1.4 46.2 1.0 NI A:NI202 1.7 23.8 1.0 F2 A:K3U201 1.9 76.7 1.0 F1 A:K3U201 2.2 43.2 1.0 NE2 A:HIS141 2.5 22.9 1.0 NE2 A:HIS145 2.7 19.8 1.0 C11 A:K3U201 2.7 47.8 1.0 CD2 A:HIS141 2.9 25.6 1.0 OE1 A:GLU142 3.0 27.9 1.0 OE2 A:GLU142 3.0 27.2 1.0 CD2 A:HIS145 3.1 18.6 1.0 OE1 A:GLN51 3.2 23.4 1.0 CD A:GLU142 3.4 24.9 1.0 NE2 A:GLN51 3.5 22.2 1.0 CD A:GLN51 3.6 23.3 1.0 CE1 A:HIS141 3.8 26.5 1.0 C3 A:K3U201 3.8 49.5 1.0 CE1 A:HIS145 3.9 25.4 1.0 SG A:CSD99 4.0 32.7 1.0 C4 A:K3U201 4.1 44.5 1.0 OD1 A:CSD99 4.2 32.1 1.0 CG A:HIS141 4.2 24.1 1.0 CG A:HIS145 4.4 18.7 1.0 ND1 A:HIS141 4.6 24.1 1.0 O A:GLY46 4.7 24.7 1.0 ND1 A:HIS145 4.8 21.1 1.0 CG A:GLU142 4.9 21.6 1.0 CG A:GLN51 4.9 21.5 1.0 CA A:CSD99 4.9 28.7 1.0 CB A:CSD99 5.0 32.3 1.0 C A:GLY46 5.0 23.2 1.0

Fluorine binding site 3 out of 3 in the K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of K3U Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:76.7 occ:1.00 F2 A:K3U201 0.0 76.7 1.0 C12 A:K3U201 1.3 46.2 1.0 F A:K3U201 1.9 23.4 1.0 C11 A:K3U201 2.1 47.8 1.0 F1 A:K3U201 2.2 43.2 1.0 OE1 A:GLN51 2.5 23.4 1.0 NE2 A:GLN51 2.9 22.2 1.0 CD A:GLN51 3.0 23.3 1.0 NI A:NI202 3.1 23.8 1.0 O A:GLY46 3.2 24.7 1.0 OE2 A:GLU142 3.4 27.2 1.0 OE1 A:GLU142 3.5 27.9 1.0 C3 A:K3U201 3.6 49.5 1.0 C A:GLY46 3.8 23.2 1.0 CA A:LEU47 3.8 17.2 1.0 CD A:GLU142 3.9 24.9 1.0 NE2 A:HIS145 4.1 19.8 1.0 N A:LEU47 4.1 19.0 1.0 CD1 A:LEU100 4.2 33.5 1.0 NE2 A:HIS141 4.3 22.9 1.0 CD1 A:LEU47 4.3 23.9 1.0 C4 A:K3U201 4.3 44.5 1.0 CD2 A:HIS145 4.4 18.6 1.0 CG A:LEU100 4.5 30.8 1.0 N A:ALA48 4.5 17.9 1.0 N A:LEU100 4.5 29.5 1.0 CG A:GLN51 4.6 21.5 1.0 CB A:LEU100 4.6 29.3 1.0 OD1 A:CSD99 4.6 32.1 1.0 C2 A:K3U201 4.6 53.9 1.0 C A:LEU47 4.6 17.5 1.0 CD2 A:HIS141 4.6 25.6 1.0 CB A:LEU47 4.7 18.9 1.0 CA A:GLY46 4.8 23.5 1.0 SG A:CSD99 4.9 32.7 1.0

I.H.Lee, L.W.Kang. Fbis Complex Structure of Peptide Deformylase From Xanthomonas Oryzae Pv. Oryzae To Be Published.