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Fluorine in PDB 4a92: Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.

Enzymatic activity of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.

All present enzymatic activity of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.:
3.4.21.98; 3.6.1.15; 3.6.4.13;

Protein crystallography data

The structure of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor., PDB code: 4a92 was solved by N.Schiering, A.D'arcy, O.Simic, J.Eder, P.Raman, D.I.Svergun, U.Bodendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.40 / 2.73
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 91.972, 110.470, 137.227, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 23.1

Other elements in 4a92:

The structure of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. (pdb code 4a92). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor., PDB code: 4a92:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 4a92

Go back to Fluorine Binding Sites List in 4a92
Fluorine binding site 1 out of 4 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1721

b:57.6
occ:1.00
 F1 A:F9K1721 0.0 57.6 1.0
C2 A:F9K1721 1.3 55.7 1.0
C3 A:F9K1721 2.4 52.3 1.0
C7 A:F9K1721 2.4 54.5 1.0
C10 A:F9K1721 3.0 49.3 1.0
OD2 A:ASP168 3.2 62.8 1.0
NE A:ARG155 3.4 33.7 1.0
CG A:ARG155 3.5 32.6 1.0
CD A:ARG155 3.6 28.7 1.0
C4 A:F9K1721 3.6 53.9 1.0
C6 A:F9K1721 3.7 53.0 1.0
CB A:ALA156 3.9 23.0 1.0
C5 A:F9K1721 4.2 53.2 1.0
CG A:ASP168 4.2 54.7 1.0
CZ A:ARG155 4.2 45.9 1.0
N9 A:F9K1721 4.3 50.5 1.0
O A:HOH2083 4.7 34.9 1.0
NH2 A:ARG155 4.7 28.5 1.0
C8 A:F9K1721 4.7 54.9 1.0
OD1 A:ASP168 4.8 59.5 1.0
CB A:ARG155 4.8 25.1 1.0
O49 A:F9K1721 5.0 33.4 1.0

Fluorine binding site 2 out of 4 in 4a92

Go back to Fluorine Binding Sites List in 4a92
Fluorine binding site 2 out of 4 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1721

b:54.9
occ:1.00
 F35 A:F9K1721 0.0 54.9 1.0
C33 A:F9K1721 1.3 48.9 1.0
C32 A:F9K1721 2.3 45.5 1.0
C34 A:F9K1721 2.3 44.5 1.0
CA A:GLY58 3.1 28.8 1.0
O A:HIS57 3.1 35.8 1.0
CG A:GLN41 3.2 55.4 1.0
C31 A:F9K1721 3.5 43.6 1.0
CB A:GLN41 3.6 41.6 1.0
C29 A:F9K1721 3.6 47.4 1.0
CD A:GLN41 3.6 84.7 1.0
C A:HIS57 3.8 32.6 1.0
N A:GLY58 3.8 28.9 1.0
OE1 A:GLN41 3.9 85.2 1.0
O A:GLY58 3.9 34.1 1.0
C A:GLY58 4.0 33.9 1.0
C30 A:F9K1721 4.1 45.9 1.0
NE2 A:GLN41 4.3 74.3 1.0
CD2 A:HIS57 4.4 25.9 1.0
CD1 A:PHE43 4.5 26.8 1.0
CE1 A:PHE43 4.6 27.0 1.0
O59 A:F9K1721 4.8 53.7 1.0
S28 A:F9K1721 4.9 51.0 1.0

Fluorine binding site 3 out of 4 in 4a92

Go back to Fluorine Binding Sites List in 4a92
Fluorine binding site 3 out of 4 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1721

b:63.2
occ:1.00
 F1 B:F9K1721 0.0 63.2 1.0
C2 B:F9K1721 1.3 61.4 1.0
C7 B:F9K1721 2.4 62.0 1.0
C3 B:F9K1721 2.4 55.8 1.0
C10 B:F9K1721 3.0 50.5 1.0
OD2 B:ASP168 3.3 81.5 1.0
NE B:ARG155 3.4 65.8 1.0
CD B:ARG155 3.4 59.4 1.0
C6 B:F9K1721 3.6 60.2 1.0
C4 B:F9K1721 3.6 55.1 1.0
CG B:ARG155 3.6 51.9 1.0
CZ B:ARG155 4.0 69.2 1.0
C5 B:F9K1721 4.2 57.0 1.0
N9 B:F9K1721 4.4 48.2 1.0
CG B:ASP168 4.5 81.4 1.0
NH2 B:ARG155 4.6 54.9 1.0
NH1 B:ARG155 4.7 45.0 1.0
CB B:ALA156 4.7 51.7 1.0
C8 B:F9K1721 4.8 50.3 1.0
CB B:ASP81 4.9 47.7 1.0
OD2 B:ASP81 5.0 58.9 1.0

Fluorine binding site 4 out of 4 in 4a92

Go back to Fluorine Binding Sites List in 4a92
Fluorine binding site 4 out of 4 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1721

b:70.4
occ:1.00
 F35 B:F9K1721 0.0 70.4 1.0
C33 B:F9K1721 1.3 68.4 1.0
C34 B:F9K1721 2.3 68.0 1.0
C32 B:F9K1721 2.3 67.2 1.0
CG B:GLN41 3.1 66.8 1.0
O B:HIS57 3.3 43.5 1.0
CA B:GLY58 3.3 37.4 1.0
CD B:GLN41 3.5 89.1 1.0
CB B:GLN41 3.5 53.9 1.0
C31 B:F9K1721 3.6 67.0 1.0
C29 B:F9K1721 3.6 69.1 1.0
OE1 B:GLN41 3.8 88.5 1.0
N B:GLY58 3.9 37.8 1.0
O B:GLY58 3.9 43.7 1.0
C B:HIS57 4.0 41.7 1.0
C30 B:F9K1721 4.0 68.7 1.0
C B:GLY58 4.1 44.1 1.0
NE2 B:GLN41 4.2 71.6 1.0
CD2 B:HIS57 4.4 41.2 1.0
CD1 B:PHE43 4.6 44.1 1.0
O59 B:F9K1721 4.7 72.0 1.0
CE1 B:PHE43 4.7 44.4 1.0
S28 B:F9K1721 4.9 70.3 1.0

Reference:

N.Schiering, A.D'arcy, F.Villard, O.Simic, M.Kamke, G.Monnet, U.Hassiepen, D.I.Svergun, R.Pulfer, J.Eder, P.Raman, U.Bodendorf. A Macrocyclic Hcv NS3/4A Protease Inhibitor Interacts with Protease and Helicase Residues in the Complex with Its Full- Length Target. Proc.Natl.Acad.Sci.Usa V. 108 21052 2011.
ISSN: ISSN 0027-8424
PubMed: 22160684
DOI: 10.1073/PNAS.1110534108
Page generated: Wed Jul 31 23:57:31 2024

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