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

Protein crystallography data

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

Other elements in 3oyh:

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:

Magnesium (Mg) 3 atoms
Zinc (Zn) 1 atom
Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine 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 Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti MK0536, PDB code: 3oyh:

Fluorine binding site 1 out of 1 in 3oyh

Go back to Fluorine Binding Sites List in 3oyh
Fluorine 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 Fluorine with other atoms in the F 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:F398

b:55.4
occ:1.00
FAI A:ZYN398 0.0 55.4 1.0
CAS A:ZYN398 1.3 52.6 1.0
CAU A:ZYN398 2.3 52.7 1.0
CAK A:ZYN398 2.3 50.1 1.0
CLAJ A:ZYN398 2.7 61.3 1.0
N4 D:DC16 3.2 51.0 1.0
C4 D:DC16 3.3 49.9 1.0
CAL A:ZYN398 3.6 49.1 1.0
CAM A:ZYN398 3.6 51.9 1.0
CG A:GLN215 3.6 53.0 1.0
N1 C:DG4 3.7 57.0 1.0
N3 D:DC16 3.7 50.3 1.0
O6 C:DG4 3.7 55.6 1.0
OE1 A:GLN215 3.7 53.3 1.0
C6 C:DG4 3.8 56.5 1.0
CD A:GLN215 3.8 53.9 1.0
C5 D:DC16 3.9 49.8 1.0
CAT A:ZYN398 4.1 50.5 1.0
O C:HOH328 4.2 57.1 1.0
N A:GLN215 4.3 51.1 1.0
CG A:PRO214 4.3 52.4 1.0
C2 C:DG4 4.4 55.6 1.0
C2 D:DC16 4.5 50.0 1.0
CA A:GLN215 4.5 51.7 1.0
C5 C:DG4 4.5 55.2 1.0
O C:HOH253 4.5 49.0 1.0
C6 D:DC16 4.6 48.6 1.0
CB A:GLN215 4.6 51.9 1.0
NE2 A:GLN215 4.6 55.7 1.0
C A:PRO214 4.8 51.6 1.0
CB A:PRO214 4.8 52.3 1.0
N1 D:DC16 4.9 49.2 1.0
O A:HOH503 4.9 67.2 1.0
N2 C:DG4 4.9 54.8 1.0

Reference:

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
Page generated: Wed Jul 31 21:30:39 2024

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