Chlorine in PDB 5nak: Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine

All present enzymatic activity of Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine:
1.14.13.9;

The structure of Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine, PDB code: 5nak was solved by M.Taylor, C.G.Mowat, P.Rowland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.48 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.930, 52.620, 137.990, 90.00, 104.07, 90.00
R / Rfree (%)	18.9 / 21

The binding sites of Chlorine atom in the Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine (pdb code 5nak). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine, PDB code: 5nak:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:17.6 occ:1.00 O A:HOH832 3.0 16.4 1.0 N A:GLY323 3.2 13.5 1.0 C10 A:FAD501 3.3 14.3 1.0 N10 A:FAD501 3.3 15.5 1.0 O A:HOH849 3.3 17.9 1.0 CA A:PRO318 3.4 14.8 1.0 N A:GLN322 3.4 14.1 1.0 N1 A:FAD501 3.5 13.4 1.0 C1' A:FAD501 3.6 15.1 1.0 O A:PRO318 3.7 20.1 1.0 CA A:GLY323 3.8 13.0 1.0 C9A A:FAD501 3.8 19.1 1.0 CA A:GLY321 3.8 14.8 1.0 C4X A:FAD501 3.9 17.4 1.0 C A:PRO318 3.9 19.7 1.0 CB A:PRO318 3.9 16.7 1.0 N A:GLY321 4.0 14.3 1.0 C A:GLY321 4.0 16.3 1.0 C2 A:FAD501 4.2 15.5 1.0 C A:GLN322 4.2 15.5 1.0 O A:VAL317 4.2 16.9 1.0 C5X A:FAD501 4.3 19.4 1.0 CA A:GLN322 4.3 13.8 1.0 N5 A:FAD501 4.3 20.6 1.0 N A:PRO318 4.5 15.1 1.0 C9 A:FAD501 4.6 19.0 1.0 C4 A:FAD501 4.6 15.4 1.0 N3 A:FAD501 4.7 15.3 1.0 C A:VAL317 4.7 17.3 1.0 CG A:MET316 4.8 14.8 1.0 O2 A:FAD501 4.8 16.1 1.0 SD A:MET316 4.9 16.0 1.0 N A:PHE319 5.0 16.6 1.0

Chlorine binding site 2 out of 2 in the Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Pseudomonas Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with the Enzyme Substrate L-Kynurenine within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:20.7 occ:1.00 O B:HOH856 3.1 24.2 1.0 N B:GLY323 3.1 16.5 1.0 C10 B:FAD501 3.2 15.4 1.0 O B:HOH826 3.3 18.3 1.0 N10 B:FAD501 3.3 16.0 1.0 CA B:PRO318 3.4 20.2 1.0 N B:GLN322 3.4 19.1 1.0 N1 B:FAD501 3.4 15.0 1.0 C1' B:FAD501 3.6 15.9 1.0 O B:PRO318 3.7 26.0 1.0 CA B:GLY321 3.8 19.6 1.0 CA B:GLY323 3.8 15.8 1.0 C4X B:FAD501 3.8 17.7 1.0 C B:PRO318 3.9 25.0 1.0 CB B:PRO318 3.9 21.7 1.0 C9A B:FAD501 3.9 17.4 1.0 N B:GLY321 3.9 18.4 1.0 C B:GLY321 3.9 21.4 1.0 C2 B:FAD501 4.1 14.9 1.0 C B:GLN322 4.1 19.6 1.0 O B:VAL317 4.2 20.0 1.0 CA B:GLN322 4.3 18.5 1.0 C5X B:FAD501 4.3 16.5 1.0 N5 B:FAD501 4.3 18.1 1.0 N B:PRO318 4.5 19.5 1.0 C4 B:FAD501 4.5 17.3 1.0 N3 B:FAD501 4.6 15.2 1.0 C9 B:FAD501 4.6 17.6 1.0 O2 B:FAD501 4.7 15.6 1.0 C B:VAL317 4.7 20.9 1.0 CG B:MET316 4.8 18.2 1.0 N B:PHE319 4.9 21.1 1.0 SD B:MET316 5.0 19.9 1.0 C B:HIS320 5.0 22.5 1.0

J.P.Hutchinson, P.Rowland, M.R.D.Taylor, E.M.Christodoulou, C.Haslam, C.I.Hobbs, D.S.Holmes, P.Homes, J.Liddle, D.J.Mole, I.Uings, A.L.Walker, S.P.Webster, C.G.Mowat, C.W.Chung. Structural and Mechanistic Basis of Differentiated Inhibitors of the Acute Pancreatitis Target Kynurenine-3-Monooxygenase. Nat Commun V. 8 15827 2017.
ISSN: ESSN 2041-1723
PubMed: 28604669
DOI: 10.1038/NCOMMS15827