Chlorine in PDB 3oyh: Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536

The structure of Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536, PDB code: 3oyh was solved by S.Hare, P.Cherepanov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.92 / 2.74
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	159.030, 159.030, 123.730, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 23.6

The structure of Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536 also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Magnesium	(Mg)	3 atoms
Zinc	(Zn)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536 (pdb code 3oyh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536, PDB code: 3oyh:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl398 b:61.3 occ:1.00 CLAJ A:ZYN398 0.0 61.3 1.0 CAU A:ZYN398 1.7 52.7 1.0 CAS A:ZYN398 2.6 52.6 1.0 CAM A:ZYN398 2.7 51.9 1.0 FAI A:ZYN398 2.7 55.4 1.0 CB A:GLU221 3.3 48.5 1.0 CG A:GLU221 3.4 48.0 1.0 N2 C:DG4 3.4 54.8 1.0 O A:PRO214 3.5 51.3 1.0 C2 C:DG4 3.6 55.6 1.0 C A:PRO214 3.6 51.6 1.0 C2 D:DC16 3.7 50.0 1.0 N1 C:DG4 3.7 57.0 1.0 N3 D:DC16 3.7 50.3 1.0 N A:GLN215 3.8 51.1 1.0 CB A:PRO214 3.9 52.3 1.0 O2 D:DC16 3.9 49.3 1.0 CAK A:ZYN398 3.9 50.1 1.0 CAT A:ZYN398 4.0 50.5 1.0 CA A:GLN215 4.0 51.7 1.0 N1 D:DC16 4.1 49.2 1.0 C4 D:DC16 4.1 49.9 1.0 CD A:GLU221 4.2 50.1 1.0 CG A:PRO214 4.3 52.4 1.0 N3 C:DG4 4.3 55.0 1.0 CA A:PRO214 4.4 52.2 1.0 CAL A:ZYN398 4.4 49.1 1.0 C6 D:DC16 4.5 48.6 1.0 C5 D:DC16 4.5 49.8 1.0 C6 C:DG4 4.6 56.5 1.0 C2' D:DC16 4.7 51.0 1.0 N4 D:DC16 4.7 51.0 1.0 CG A:GLN215 4.8 53.0 1.0 C1' D:DC16 4.8 50.1 1.0 CA A:GLY218 4.8 50.8 1.0 OE1 A:GLU221 4.8 49.0 1.0 OE2 A:GLU221 4.8 52.6 1.0 CA A:GLU221 4.8 48.8 1.0 OE1 A:GLN215 4.8 53.3 1.0 CB A:GLN215 4.9 51.9 1.0 C4 C:DG4 5.0 54.8 1.0

S.Hare, A.M.Vos, R.F.Clayton, J.W.Thuring, M.D.Cummings, P.Cherepanov. Molecular Mechanisms of Retroviral Integrase Inhibition and the Evolution of Viral Resistance. Proc.Natl.Acad.Sci.Usa V. 107 20057 2010.
ISSN: ISSN 0027-8424
PubMed: 21030679
DOI: 10.1073/PNAS.1010246107