Chlorine in PDB 3nj8: Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor

All present enzymatic activity of Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor:
1.3.1.9;

The structure of Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor, PDB code: 3nj8 was solved by S.P.Muench, S.N.Ruzheinikov, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	78.256, 78.256, 189.077, 90.00, 90.00, 120.00
R / Rfree (%)	27.4 / 32.2

The binding sites of Chlorine atom in the Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor (pdb code 3nj8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor, PDB code: 3nj8:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:39.3 occ:1.00 CL16 A:NJ8501 0.0 39.3 1.0 C9 A:NJ8501 1.8 39.1 1.0 C10 A:NJ8501 2.7 39.4 1.0 C8 A:NJ8501 2.8 38.8 1.0 O3 A:NAD316 3.0 35.8 1.0 O7 A:NJ8501 3.1 38.4 1.0 C3D A:NAD316 3.3 34.6 1.0 C5B A:NAD316 3.3 36.9 1.0 C2D A:NAD316 3.6 34.6 1.0 CB A:ALA231 3.7 36.0 1.0 O5B A:NAD316 3.7 36.1 1.0 C5D A:NAD316 3.7 35.1 1.0 O A:ALA129 3.9 37.6 1.0 O1N A:NAD316 4.0 35.8 1.0 CB A:ALA129 4.0 37.5 1.0 PN A:NAD316 4.0 36.0 1.0 N A:ALA129 4.0 37.6 1.0 C11 A:NJ8501 4.0 39.5 1.0 C13 A:NJ8501 4.1 39.0 1.0 C4D A:NAD316 4.1 34.6 1.0 PA A:NAD316 4.1 35.7 1.0 O5D A:NAD316 4.2 35.9 1.0 O2D A:NAD316 4.3 34.7 1.0 O3D A:NAD316 4.3 34.7 1.0 CA A:ALA129 4.4 37.5 1.0 C5 A:NJ8501 4.4 38.0 1.0 C A:ALA129 4.4 37.5 1.0 C4B A:NAD316 4.5 37.6 1.0 C12 A:NJ8501 4.6 39.2 1.0 C A:LEU128 4.6 37.7 1.0 O4B A:NAD316 4.8 37.9 1.0 O4D A:NAD316 4.8 34.3 1.0 C1D A:NAD316 4.8 34.4 1.0 CA A:LEU128 4.9 37.6 1.0 O17 A:NJ8501 5.0 38.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of T. Gondii Enoyl Acyl Carrier Protein Reductase with Bound Triclosan Like Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl501 b:39.2 occ:1.00 CL16 B:NJ8501 0.0 39.2 1.0 C9 B:NJ8501 1.8 38.5 1.0 C10 B:NJ8501 2.7 38.4 1.0 C8 B:NJ8501 2.8 38.4 1.0 O7 B:NJ8501 3.0 38.5 1.0 O5B B:NAD316 3.3 35.5 1.0 C5B B:NAD316 3.3 36.6 1.0 O1N B:NAD316 3.4 33.4 1.0 C3D B:NAD316 3.5 33.7 1.0 CB B:ALA231 3.6 37.2 1.0 O B:ALA129 3.6 36.7 1.0 O5D B:NAD316 3.7 33.5 1.0 C2D B:NAD316 3.7 33.8 1.0 N B:ALA129 3.9 36.4 1.0 C11 B:NJ8501 4.0 38.2 1.0 PN B:NAD316 4.1 33.4 1.0 C13 B:NJ8501 4.1 38.4 1.0 CB B:ALA129 4.1 36.4 1.0 C5D B:NAD316 4.1 33.6 1.0 O3 B:NAD316 4.3 33.9 1.0 C5 B:NJ8501 4.3 38.4 1.0 C B:ALA129 4.3 36.6 1.0 CA B:ALA129 4.3 36.5 1.0 O3D B:NAD316 4.4 33.8 1.0 PA B:NAD316 4.4 34.3 1.0 O2D B:NAD316 4.4 33.7 1.0 C4D B:NAD316 4.4 33.7 1.0 C12 B:NJ8501 4.6 38.4 1.0 C4B B:NAD316 4.7 37.5 1.0 O1A B:NAD316 4.7 34.2 1.0 C B:LEU128 4.8 36.2 1.0 C4 B:NJ8501 4.9 38.1 1.0 CA B:ALA231 5.0 37.2 1.0 O4B B:NAD316 5.0 38.1 1.0

S.K.Tipparaju, S.P.Muench, E.J.Mui, S.N.Ruzheinikov, J.Z.Lu, S.L.Hutson, M.J.Kirisits, S.T.Prigge, C.W.Roberts, F.L.Henriquez, A.P.Kozikowski, D.W.Rice, R.L.Mcleod. Identification and Development of Novel Inhibitors of Toxoplasma Gondii Enoyl Reductase. J.Med.Chem. V. 53 6287 2010.
ISSN: ISSN 0022-2623
PubMed: 20698542
DOI: 10.1021/JM9017724