Bromine in PDB 6qdg: Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169:
2.3.1.97;

The structure of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169, PDB code: 6qdg was solved by J.A.Brannigan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.75 / 1.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.598, 91.202, 53.344, 90.00, 113.96, 90.00
R / Rfree (%)	18.6 / 25.4

The structure of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Bromine atom in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 (pdb code 6qdg). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169, PDB code: 6qdg:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1003 b:86.3 occ:0.50 BR A:HXN1003 0.0 86.3 0.5 BR A:HXN1003 0.1 93.3 0.5 C14 A:HXN1003 1.9 72.0 0.5 C14 A:HXN1003 1.9 75.7 0.5 C13 A:HXN1003 2.8 67.7 0.5 C13 A:HXN1003 2.8 70.6 0.5 C15 A:HXN1003 2.9 66.3 0.5 C15 A:HXN1003 2.9 69.7 0.5 O A:ASP396 3.1 51.4 1.0 O A:HOH1271 3.1 53.7 1.0 N A:ASP396 3.5 46.4 1.0 CA A:GLY395 3.8 34.5 1.0 CB A:TYR217 3.9 28.9 0.5 CB A:TYR217 4.0 23.3 0.5 C A:ASP396 4.0 50.0 1.0 C A:GLY395 4.0 44.4 1.0 C12 A:HXN1003 4.1 63.1 0.5 C12 A:HXN1003 4.1 65.2 0.5 CG A:TYR217 4.2 34.0 0.5 C16 A:HXN1003 4.2 63.9 0.5 C16 A:HXN1003 4.2 66.6 0.5 CD1 A:TYR217 4.2 35.7 0.5 CA A:ASP396 4.3 50.7 1.0 CG A:TYR217 4.6 23.6 0.5 C9 A:HXN1003 4.6 71.5 0.5 C9 A:HXN1003 4.7 66.5 0.5 C17 A:HXN1003 4.7 61.1 0.5 C17 A:HXN1003 4.7 63.5 0.5 CB A:ASP396 4.8 58.4 1.0 CD2 A:TYR217 4.9 34.6 0.5 N A:GLY395 4.9 38.5 1.0 CD1 A:TYR217 5.0 23.8 0.5

Bromine binding site 2 out of 2 in the Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Leishmania Major N-Myristoyltransferase in Complex with Quinazoline Inhibitor Imp-0000169 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1003 b:93.3 occ:0.50 BR A:HXN1003 0.0 93.3 0.5 BR A:HXN1003 0.1 86.3 0.5 C14 A:HXN1003 1.9 72.0 0.5 C14 A:HXN1003 1.9 75.7 0.5 C13 A:HXN1003 2.8 67.7 0.5 C13 A:HXN1003 2.8 70.6 0.5 C15 A:HXN1003 2.9 66.3 0.5 C15 A:HXN1003 2.9 69.7 0.5 O A:HOH1271 3.1 53.7 1.0 O A:ASP396 3.1 51.4 1.0 N A:ASP396 3.6 46.4 1.0 CA A:GLY395 3.9 34.5 1.0 CB A:TYR217 4.0 28.9 0.5 C A:ASP396 4.1 50.0 1.0 C A:GLY395 4.1 44.4 1.0 CB A:TYR217 4.1 23.3 0.5 C12 A:HXN1003 4.1 63.1 0.5 C12 A:HXN1003 4.1 65.2 0.5 C16 A:HXN1003 4.2 63.9 0.5 C16 A:HXN1003 4.2 66.6 0.5 CG A:TYR217 4.2 34.0 0.5 CA A:ASP396 4.3 50.7 1.0 CD1 A:TYR217 4.3 35.7 0.5 C9 A:HXN1003 4.6 71.5 0.5 CG A:TYR217 4.6 23.6 0.5 C9 A:HXN1003 4.7 66.5 0.5 C17 A:HXN1003 4.7 61.1 0.5 C17 A:HXN1003 4.7 63.5 0.5 CB A:ASP396 4.8 58.4 1.0 N A:GLY395 5.0 38.5 1.0 CD2 A:TYR217 5.0 34.6 0.5

J.A.Brannigan, J.A.Brannigan. N/A N/A.