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

Protein crystallography data

The structure of Crystal Structure of the Prototype Foamy Virus (Pfv) Intasome in Complex with Magnesium and the Insti Pica, PDB code: 3oyc 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) 38.80 / 2.66
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 159.960, 159.960, 123.770, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.6

Other elements in 3oyc:

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

Magnesium (Mg) 2 atoms
Zinc (Zn) 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 Pica (pdb code 3oyc). 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 Pica, PDB code: 3oyc:

Fluorine binding site 1 out of 1 in 3oyc

Go back to Fluorine Binding Sites List in 3oyc
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 Pica


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 Pica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F398

b:43.8
occ:1.00
FAC A:ZZW398 0.0 43.8 1.0
CAR A:ZZW398 1.3 39.6 1.0
CAG A:ZZW398 2.3 37.7 1.0
CAF A:ZZW398 2.4 37.9 1.0
N1 C:DG4 2.9 40.4 1.0
C6 C:DG4 3.1 40.4 1.0
C2 C:DG4 3.3 39.3 1.0
CA A:GLN215 3.4 41.8 1.0
N A:GLN215 3.5 40.7 1.0
C5 C:DG4 3.5 39.1 1.0
O6 C:DG4 3.5 40.4 1.0
CG A:GLN215 3.5 46.3 1.0
CAI A:ZZW398 3.6 39.2 1.0
CAH A:ZZW398 3.6 38.0 1.0
C4 C:DG4 3.8 39.8 1.0
N3 C:DG4 3.8 38.8 1.0
OE1 A:GLN215 3.9 50.3 1.0
CD A:GLN215 3.9 51.7 1.0
N2 C:DG4 4.0 36.8 1.0
N3 D:DC16 4.0 36.0 1.0
CB A:GLN215 4.0 42.5 1.0
C A:PRO214 4.0 40.5 1.0
CAS A:ZZW398 4.1 40.1 1.0
N4 D:DC16 4.1 32.6 1.0
C4 D:DC16 4.2 33.9 1.0
O A:PRO214 4.3 40.1 1.0
N7 C:DG4 4.4 38.4 1.0
C2 D:DC16 4.7 38.2 1.0
CB A:PRO214 4.7 40.4 1.0
N9 C:DG4 4.7 40.7 1.0
CG A:PRO214 4.8 40.4 1.0
C A:GLN215 4.8 41.8 1.0
NE2 A:GLN215 4.9 55.8 1.0
CA A:PRO214 4.9 40.5 1.0
C8 C:DG4 5.0 39.4 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: Sun Dec 13 11:52:45 2020

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