Fluorine in PDB 4xjr: The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed

All present enzymatic activity of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed:
3.2.1.18;

The structure of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed, PDB code: 4xjr was solved by L.Dirr, I.El-Deeb, P.Guillon, C.Carroux, L.Chavas, M.Von Itzstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.850, 98.303, 103.261, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 29.8

The structure of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Fluorine atom in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed (pdb code 4xjr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed, PDB code: 4xjr:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed within 5.0Å range: probe atom residue distance (Å) B Occ A:F606 b:48.9 occ:1.00 F3 A:OEL606 0.0 48.9 1.0 C3 A:OEL606 1.4 48.6 1.0 C4 A:OEL606 2.3 49.1 1.0 NH2 A:ARG192 2.4 55.4 1.0 C2 A:OEL606 2.4 49.1 1.0 OH A:TYR530 2.6 45.4 1.0 N4 A:OEL606 2.7 51.0 1.0 O1A A:OEL606 2.8 48.0 1.0 CZ A:TYR530 2.9 38.5 1.0 C1 A:OEL606 3.0 49.4 1.0 CE2 A:TYR530 3.1 36.5 1.0 CZ A:ARG192 3.4 53.9 1.0 O6 A:OEL606 3.6 49.4 1.0 C5 A:OEL606 3.7 47.0 1.0 NE A:ARG192 3.7 52.2 1.0 CG2 A:THR193 3.7 39.2 1.0 N41 A:OEL606 3.8 52.4 1.0 CE1 A:TYR530 3.9 35.4 1.0 C6 A:OEL606 4.1 48.6 1.0 CD2 A:TYR530 4.2 34.6 1.0 O1B A:OEL606 4.2 46.4 1.0 NH1 A:ARG192 4.5 55.5 1.0 CD1 A:TYR530 4.7 34.9 1.0 OE2 A:GLU409 4.8 32.3 1.0 N5 A:OEL606 4.8 43.7 1.0 N42 A:OEL606 4.8 54.6 1.0 CG A:TYR530 4.9 33.5 1.0

Fluorine binding site 2 out of 2 in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed within 5.0Å range: probe atom residue distance (Å) B Occ B:F606 b:49.6 occ:1.00 F3 B:OEL606 0.0 49.6 1.0 C3 B:OEL606 1.4 47.8 1.0 C2 B:OEL606 2.4 47.2 1.0 C4 B:OEL606 2.4 48.2 1.0 O1A B:OEL606 2.6 44.8 1.0 NH2 B:ARG192 2.7 58.8 1.0 N4 B:OEL606 2.8 52.1 1.0 C1 B:OEL606 2.9 45.7 1.0 N41 B:OEL606 2.9 61.5 1.0 OH B:TYR530 2.9 42.8 1.0 CZ B:TYR530 3.2 37.9 1.0 N42 B:OEL606 3.3 63.4 1.0 CE2 B:TYR530 3.4 36.6 1.0 O6 B:OEL606 3.6 47.9 1.0 CZ B:ARG192 3.6 58.7 1.0 C5 B:OEL606 3.7 47.9 1.0 NE B:ARG192 3.8 54.9 1.0 CE1 B:TYR530 4.0 35.1 1.0 O1B B:OEL606 4.1 45.0 1.0 C6 B:OEL606 4.2 47.6 1.0 CG2 B:THR193 4.3 36.7 1.0 CD2 B:TYR530 4.3 35.7 1.0 CD1 B:TYR530 4.8 34.5 1.0 N5 B:OEL606 4.8 47.2 1.0 NH1 B:ARG192 4.9 59.5 1.0 CG B:TYR530 5.0 34.9 1.0

L.Dirr, I.M.El-Deeb, P.Guillon, C.J.Carroux, L.M.G.Chavas, M.Von Itzstein. The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed. Angew.Chem.Int.Ed.Engl. 2015.
ISSN: ESSN 1521-3773