Chlorine in PDB 4a95: Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor

All present enzymatic activity of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor:
2.3.1.97;

The structure of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor, PDB code: 4a95 was solved by V.Goncalves, J.A.Brannigan, D.Whalley, K.H.Ansell, B.Saxty, A.A.Holder, A.J.Wilkinson, E.W.Tate, R.J.Leatherbarrow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.08 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.490, 121.560, 179.010, 90.00, 90.00, 90.00
R / Rfree (%)	18.649 / 23.596

The structure of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor (pdb code 4a95). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor, PDB code: 4a95:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1411 b:12.3 occ:1.00 NZ A:LYS180 3.3 10.0 1.0 CE2 A:TYR65 3.7 9.6 1.0 CD A:LYS180 3.9 10.2 1.0 CE A:LYS180 4.1 9.5 1.0 OH A:TYR65 4.6 11.3 1.0 CD2 A:TYR65 4.6 8.8 1.0 CZ A:TYR65 4.7 9.4 1.0

Chlorine binding site 2 out of 3 in the Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1412 b:12.7 occ:1.00 NZ B:LYS180 3.2 12.6 1.0 CE1 B:TYR65 3.7 12.1 1.0 CD B:LYS180 4.0 9.3 1.0 CE B:LYS180 4.1 10.8 1.0 OH B:TYR65 4.5 11.4 1.0 CZ B:TYR65 4.6 12.8 1.0 CD1 B:TYR65 4.6 11.8 1.0

Chlorine binding site 3 out of 3 in the Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Plasmodium Vivax N-Myristoyltransferase with Quinoline Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1411 b:13.0 occ:1.00 O C:HOH2296 3.2 17.9 1.0 NH2 C:ARG358 3.2 11.3 1.0 N C:LEU248 3.3 13.1 1.0 O C:HOH2286 3.3 18.7 1.0 CA C:THR247 3.6 11.8 1.0 O C:HOH2404 3.8 14.2 1.0 C C:THR247 4.0 12.3 1.0 CG2 C:THR247 4.0 11.7 1.0 CG C:LEU248 4.0 12.3 1.0 O C:ASP246 4.1 13.0 1.0 CB C:LEU248 4.1 12.7 1.0 CZ C:ARG358 4.2 12.3 1.0 CD1 C:LEU248 4.2 12.4 1.0 CB C:THR247 4.3 11.9 1.0 NH1 C:ARG358 4.3 11.8 1.0 CA C:LEU248 4.3 12.7 1.0 OG1 C:THR247 4.6 14.2 1.0 N C:THR247 4.7 11.5 1.0 C C:ASP246 4.8 11.9 1.0 O C:LEU248 4.9 13.8 1.0

V.Goncalves, J.A.Brannigan, D.Whalley, K.H.Ansell, B.Saxty, A.A.Holder, A.J.Wilkinson, E.W.Tate, R.J.Leatherbarrow. Discovery of Plasmodium Vivax N-Myristoyltransferase Inhibitors: Screening, Synthesis, and Structural Characterization of Their Binding Mode. J.Med.Chem. V. 55 3578 2012.
ISSN: ISSN 0022-2623
PubMed: 22439843
DOI: 10.1021/JM300040P