Chlorine in PDB 6eu5: Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor

All present enzymatic activity of Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor:
2.3.1.97;

The structure of Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor, PDB code: 6eu5 was solved by R.Brenk, J.Kehrein, C.Kersten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.75 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.770, 90.590, 53.420, 90.00, 114.14, 90.00
R / Rfree (%)	16.9 / 20.3

The binding sites of Chlorine atom in the Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor (pdb code 6eu5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor, PDB code: 6eu5:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:45.2 occ:1.00 CL1 A:BXN502 0.0 45.2 1.0 C15 A:BXN502 1.8 39.1 1.0 C17 A:BXN502 2.7 35.8 1.0 C14 A:BXN502 2.8 36.5 1.0 O13 A:BXN502 3.1 37.8 1.0 S11 A:BXN502 3.2 35.2 1.0 O A:HOH688 3.3 24.6 1.0 C10 A:BXN502 3.4 31.5 1.0 N09 A:BXN502 3.4 30.1 1.0 N A:GLY387 3.9 18.6 1.0 CA A:GLY387 3.9 19.2 1.0 C07 A:BXN502 4.0 21.5 1.0 C18 A:BXN502 4.0 33.4 1.0 C32 A:BXN502 4.1 35.7 1.0 C08 A:BXN502 4.4 25.1 1.0 CB A:ASP386 4.5 32.3 1.0 C06 A:BXN502 4.6 21.1 1.0 C31 A:BXN502 4.6 34.4 1.0 C A:ASP386 4.7 23.3 1.0 O12 A:BXN502 4.7 36.9 1.0 O A:HOH814 4.8 43.2 1.0

Chlorine binding site 2 out of 2 in the Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Leishmania Major N-Myristoyltransferase with Bound Myristoyl-Coa and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:36.8 occ:1.00 CL2 A:BXN502 0.0 36.8 1.0 C32 A:BXN502 1.8 35.7 1.0 C31 A:BXN502 2.7 34.4 1.0 C14 A:BXN502 2.8 36.5 1.0 O12 A:BXN502 2.9 36.9 1.0 OH A:TYR335 3.2 20.9 1.0 S11 A:BXN502 3.4 35.2 1.0 CZ A:PHE80 3.7 20.9 1.0 CE2 A:TYR335 3.9 17.6 1.0 CE1 A:PHE80 3.9 20.2 1.0 CE2 A:TYR207 3.9 19.9 1.0 CZ A:TYR335 4.0 18.2 1.0 C18 A:BXN502 4.0 33.4 1.0 ND2 A:ASN366 4.1 22.6 1.0 C15 A:BXN502 4.1 39.1 1.0 CZ A:TYR207 4.3 19.2 1.0 CD2 A:TYR207 4.3 17.7 1.0 C08 A:BXN502 4.3 25.1 1.0 N09 A:BXN502 4.5 30.1 1.0 C06 A:BXN502 4.5 21.1 1.0 OH A:TYR207 4.5 19.6 1.0 C17 A:BXN502 4.5 35.8 1.0 O13 A:BXN502 4.6 37.8 1.0 C02 A:BXN502 4.7 25.2 1.0 CG A:ASN366 4.9 18.2 1.0 C07 A:BXN502 4.9 21.5 1.0 N04 A:BXN502 4.9 20.6 1.0 CE2 A:PHE80 4.9 20.4 1.0 CE1 A:TYR207 5.0 17.7 1.0

C.Kersten, E.Fleischer, J.Kehrein, C.Borek, E.Jaenicke, C.Sotriffer, R.Brenk. How to Design Selective Ligands For Highly Conserved Binding Sites: A Case Study Usingn-Myristoyltransferases As A Model System. J.Med.Chem. 2019.
ISSN: ISSN 0022-2623
PubMed: 31423787
DOI: 10.1021/ACS.JMEDCHEM.9B00586