Bromine in PDB 1w6h: Novel Plasmepsin II-Inhibitor Complex

All present enzymatic activity of Novel Plasmepsin II-Inhibitor Complex:
3.4.23.39;

The structure of Novel Plasmepsin II-Inhibitor Complex, PDB code: 1w6h was solved by J.Lindberg, P.-O.Johansson, A.Rosenquist, I.Kvarnstroem, L.Vrang, B.Samuelsson, T.Unge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	84.51 / 2.24
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.210, 77.614, 84.237, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 24.6

The binding sites of Bromine atom in the Novel Plasmepsin II-Inhibitor Complex (pdb code 1w6h). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Novel Plasmepsin II-Inhibitor Complex, PDB code: 1w6h:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Novel Plasmepsin II-Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Novel Plasmepsin II-Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1330 b:69.8 occ:1.00 BR A:TIT1330 0.0 69.8 1.0 C25 A:TIT1330 1.5 61.5 1.0 C26 A:TIT1330 2.6 58.8 1.0 C24 A:TIT1330 2.6 59.3 1.0 CB A:THR114 3.3 35.5 1.0 O A:PHE111 3.4 32.3 1.0 CG2 A:THR114 3.5 36.3 1.0 CD2 A:PHE111 3.6 34.0 1.0 O A:HOH2045 3.6 41.5 1.0 CG A:PHE111 3.7 35.0 1.0 C27 A:TIT1330 3.9 54.2 1.0 C23 A:TIT1330 3.9 54.4 1.0 CE2 A:PHE111 4.0 35.4 1.0 OG1 A:THR114 4.0 37.2 1.0 O A:SER79 4.1 37.8 1.0 C A:PHE111 4.1 33.2 1.0 CA A:PHE111 4.1 33.6 1.0 CD1 A:PHE111 4.2 35.3 1.0 CB A:PHE111 4.2 33.9 1.0 C16 A:TIT1330 4.4 45.8 1.0 CZ A:PHE111 4.4 35.3 1.0 C22 A:TIT1330 4.4 51.4 1.0 CE1 A:PHE111 4.5 35.7 1.0 CA A:THR114 4.6 34.9 1.0 C15 A:TIT1330 4.6 45.8 1.0 N A:TYR115 4.7 33.3 1.0 OG A:SER79 4.9 38.0 1.0 C A:THR114 4.9 33.6 1.0

Bromine binding site 2 out of 2 in the Novel Plasmepsin II-Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Novel Plasmepsin II-Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1330 b:70.0 occ:1.00 BR B:TIT1330 0.0 70.0 1.0 C25 B:TIT1330 1.5 60.7 1.0 C26 B:TIT1330 2.5 58.6 1.0 C24 B:TIT1330 2.5 57.6 1.0 O B:PHE111 3.4 31.4 1.0 CB B:THR114 3.4 36.8 1.0 CD2 B:PHE111 3.6 33.3 1.0 CG B:PHE111 3.8 32.3 1.0 CG2 B:THR114 3.8 37.9 1.0 C27 B:TIT1330 3.9 53.1 1.0 C23 B:TIT1330 3.9 52.5 1.0 CE2 B:PHE111 3.9 33.3 1.0 OG1 B:THR114 3.9 39.0 1.0 O B:SER79 4.0 37.7 1.0 C B:PHE111 4.0 32.4 1.0 CA B:PHE111 4.1 32.5 1.0 CD1 B:PHE111 4.2 33.9 1.0 CB B:PHE111 4.2 32.5 1.0 C16 B:TIT1330 4.3 45.5 1.0 CZ B:PHE111 4.3 33.0 1.0 C22 B:TIT1330 4.4 50.1 1.0 CE1 B:PHE111 4.5 32.8 1.0 C15 B:TIT1330 4.6 45.6 1.0 CA B:THR114 4.6 36.2 1.0 N B:TYR115 4.7 34.7 1.0 OG B:SER79 4.8 40.1 1.0 C B:THR114 4.9 35.4 1.0 N B:THR114 5.0 35.1 1.0

J.Lindberg, P.-O.Johansson, A.Rosenquist, I.Kvarnstroem, L.Vrang, B.Samuelsson, T.Unge. Structural Study of A Novel Inhibitor with Bulky P1 Side Chain in Complex with Plasmepsin II -Implications For Drug Design To Be Published.