Chlorine in PDB 1qrd: Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex

All present enzymatic activity of Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex:
1.6.99.2;

The structure of Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex, PDB code: 1qrd was solved by R.Li, M.A.Bianchet, P.Talalay, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.40
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.000, 107.000, 88.400, 90.00, 92.60, 90.00
R / Rfree (%)	18.8 / n/a

The binding sites of Chlorine atom in the Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex (pdb code 1qrd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex, PDB code: 1qrd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl275 b:29.5 occ:1.00 CL A:CBD275 0.0 29.5 1.0 CC2 A:CBD275 1.9 25.5 1.0 NC1 A:CBD275 2.8 24.5 1.0 NC3 A:CBD275 2.9 25.0 1.0 C5M A:DQN276 3.0 42.6 1.0 C6M A:DQN276 3.1 42.8 1.0 C5 A:DQN276 3.6 42.6 1.0 C6 A:DQN276 3.6 42.4 1.0 CA A:GLY150 3.8 14.3 1.0 N A:GLY150 4.0 14.6 1.0 CC6 A:CBD275 4.1 24.2 1.0 CC4 A:CBD275 4.1 24.0 1.0 C A:GLY149 4.4 15.3 1.0 CE A:MET154 4.4 15.7 1.0 SD A:MET154 4.4 16.4 1.0 CE1 A:HIS161 4.4 11.0 1.0 NC5 A:CBD275 4.6 23.8 1.0 O A:GLY149 4.7 14.5 1.0 O2 A:FAD274 4.7 16.9 1.0 C4 A:DQN276 4.8 42.1 1.0 C1 A:DQN276 4.9 41.6 1.0 CB3 A:CBD275 5.0 23.5 1.0

Chlorine binding site 2 out of 2 in the Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Quinone Reductase/Fad/Cibacron Blue/Duroquinone Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl275 b:27.9 occ:1.00 CL B:CBD275 0.0 27.9 1.0 CC2 B:CBD275 1.9 25.2 1.0 NC1 B:CBD275 2.8 24.7 1.0 NC3 B:CBD275 2.9 24.9 1.0 C6M B:DQN276 3.0 45.6 1.0 C5M B:DQN276 3.1 46.1 1.0 C6 B:DQN276 3.5 45.4 1.0 C5 B:DQN276 3.5 45.5 1.0 CA B:GLY150 3.8 15.7 1.0 N B:GLY150 3.9 16.4 1.0 CC6 B:CBD275 4.1 25.1 1.0 CC4 B:CBD275 4.2 24.4 1.0 SD B:MET154 4.4 18.1 1.0 CE1 B:HIS161 4.4 15.2 1.0 C B:GLY149 4.5 17.1 1.0 CE B:MET154 4.5 17.2 1.0 NC5 B:CBD275 4.7 24.2 1.0 C1 B:DQN276 4.8 44.7 1.0 C4 B:DQN276 4.8 44.9 1.0 CB3 B:CBD275 4.8 26.5 1.0 O2 B:FAD274 4.8 19.9 1.0 O B:GLY149 4.9 17.4 1.0

R.Li, M.A.Bianchet, P.Talalay, L.M.Amzel. The Three-Dimensional Structure of Nad(P)H:Quinone Reductase, A Flavoprotein Involved in Cancer Chemoprotection and Chemotherapy: Mechanism of the Two-Electron Reduction. Proc.Natl.Acad.Sci.Usa V. 92 8846 1995.
ISSN: ISSN 0027-8424
PubMed: 7568029
DOI: 10.1073/PNAS.92.19.8846