Bromine in PDB 6fy4: Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide

All present enzymatic activity of Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide:
1.6.5.2;

The structure of Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide, PDB code: 6fy4 was solved by K.Gruber, A.Hromic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.75 / 2.76
Space group	P 31 1 2
Cell size a, b, c (Å), α, β, γ (°)	121.369, 121.369, 158.252, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 29

The binding sites of Bromine atom in the Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide (pdb code 6fy4). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide, PDB code: 6fy4:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:71.3 occ:0.49 BR1 A:EAW302 0.0 71.3 0.5 C6 A:EAW302 1.7 52.1 0.5 C2 A:EAW302 1.9 52.3 0.5 C1 A:EAW302 2.5 52.1 0.5 N1 A:EAW302 2.8 52.0 0.5 C5 A:EAW302 2.8 47.5 0.5 OH A:TYR127 2.8 54.6 1.0 C3 A:EAW302 2.9 52.4 0.5 O1 A:EAW302 2.9 55.9 0.5 C1 A:EAW302 2.9 51.9 0.5 S1 A:EAW302 3.0 63.0 0.5 N5 A:EAW302 3.0 63.7 0.5 N1 A:EAW302 3.1 51.6 0.5 C9A B:FAD301 3.6 28.7 1.0 C9 B:FAD301 3.7 28.6 1.0 C10 A:EAW302 3.8 59.5 0.5 C2 A:EAW302 3.8 52.2 0.5 C7 A:EAW302 3.8 56.3 0.5 N10 B:FAD301 3.9 29.8 1.0 CZ A:TYR127 3.9 41.5 1.0 C4 A:EAW302 4.0 48.3 0.5 CB A:PRO69 4.0 44.9 1.0 C5X B:FAD301 4.1 32.3 1.0 C1' B:FAD301 4.2 35.0 1.0 CG A:PRO69 4.2 47.4 1.0 C4 A:EAW302 4.2 47.9 0.5 C6 A:EAW302 4.2 51.6 0.5 C8 B:FAD301 4.2 28.7 1.0 CE2 A:TYR127 4.3 40.3 1.0 C3 A:EAW302 4.4 50.0 0.5 O2 A:EAW302 4.5 57.7 0.5 C10 B:FAD301 4.5 35.0 1.0 C6 B:FAD301 4.6 31.4 1.0 C7 B:FAD301 4.7 29.1 1.0 C5 A:EAW302 4.7 47.9 0.5 C8 A:EAW302 4.8 57.4 0.5 S1 A:EAW302 4.8 56.7 0.5 N5 B:FAD301 4.8 26.9 1.0 C9 A:EAW302 5.0 59.0 0.5 C4X B:FAD301 5.0 30.3 1.0 C8M B:FAD301 5.0 23.5 1.0 CE1 A:TYR127 5.0 39.5 1.0

Bromine binding site 2 out of 2 in the Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of Human Nad(P) H:Quinone Oxidoreductase in Complex with N- (2-Bromophenyl)Pyrrolidine-1-Sulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:65.4 occ:0.51 BR1 A:EAW302 0.0 65.4 0.5 O2 A:EAW302 1.7 54.7 0.5 C2 A:EAW302 1.9 52.2 0.5 C6 A:EAW302 1.9 51.6 0.5 S1 A:EAW302 2.2 56.7 0.5 C7 A:EAW302 2.3 56.5 0.5 N5 A:EAW302 2.5 61.7 0.5 C1 A:EAW302 2.5 51.9 0.5 N1 A:EAW302 2.6 51.6 0.5 C3 A:EAW302 2.8 50.0 0.5 C1 A:EAW302 2.9 52.1 0.5 C5 A:EAW302 3.1 47.9 0.5 N1 A:EAW302 3.1 52.0 0.5 C10 A:EAW302 3.7 54.6 0.5 O1 A:EAW302 3.7 53.1 0.5 C8 A:EAW302 3.8 50.0 0.5 C2 B:FAD301 3.8 29.6 1.0 C2 A:EAW302 3.9 52.3 0.5 O2 B:FAD301 3.9 33.5 1.0 NE2 B:HIS162 4.0 37.8 1.0 N1 B:FAD301 4.0 33.1 1.0 N B:GLY151 4.1 35.2 1.0 C4 A:EAW302 4.2 48.3 0.5 C6 A:EAW302 4.2 52.1 0.5 N3 B:FAD301 4.2 26.6 1.0 C4 A:EAW302 4.3 47.9 0.5 CA B:GLY151 4.4 35.5 1.0 C9 A:EAW302 4.4 53.1 0.5 OH B:TYR156 4.4 30.9 1.0 C10 B:FAD301 4.6 35.0 1.0 C3 A:EAW302 4.6 52.4 0.5 O2 A:EAW302 4.6 57.7 0.5 S1 A:EAW302 4.6 63.0 0.5 C5 A:EAW302 4.7 47.5 0.5 C B:GLY150 4.7 36.7 1.0 C4 B:FAD301 4.8 32.5 1.0 CD2 B:HIS162 4.9 34.6 1.0 CE1 B:HIS162 4.9 32.5 1.0 CA B:GLY150 4.9 39.3 1.0 C4X B:FAD301 5.0 30.3 1.0

K.Gruber, A.Hromic, P.Macheroux, W.-D.Lienhart, E.Strandback. Structure of NOQ1 in Complex with N-(2-Bromophenyl)Pyrrolidine-1-Sulfonamide To Be Published.