Fluorine in PDB 7mmi: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23

All present enzymatic activity of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23:
3.4.21.98;

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23, PDB code: 7mmi was solved by J.Zephyr, C.A.Schiffer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.11 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.166, 58.582, 59.599, 90, 90, 90
R / Rfree (%)	17.2 / 20.8

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23 (pdb code 7mmi). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23, PDB code: 7mmi:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23


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 Hcv NS3/4A D168A Protease in Complex with NR02-23 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1201 b:34.2 occ:1.00 F51 A:ZJV1201 0.0 34.2 1.0 C50 A:ZJV1201 1.4 29.5 1.0 F53 A:ZJV1201 2.2 32.0 1.0 F52 A:ZJV1201 2.3 38.2 1.0 C48 A:ZJV1201 2.3 23.9 1.0 H481 A:ZJV1201 2.6 28.7 1.0 O42 A:ZJV1201 2.7 19.7 1.0 C41 A:ZJV1201 3.2 17.4 1.0 O43 A:ZJV1201 3.4 18.8 1.0 C49 A:ZJV1201 3.7 28.5 1.0 H491 A:ZJV1201 3.8 34.2 1.0 H492 A:ZJV1201 4.1 34.2 1.0 N40 A:ZJV1201 4.1 15.6 1.0 H401 A:ZJV1201 4.3 18.8 1.0 H493 A:ZJV1201 4.3 34.2 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1201 b:38.2 occ:1.00 F52 A:ZJV1201 0.0 38.2 1.0 C50 A:ZJV1201 1.4 29.5 1.0 F53 A:ZJV1201 2.2 32.0 1.0 F51 A:ZJV1201 2.3 34.2 1.0 H491 A:ZJV1201 2.3 34.2 1.0 C48 A:ZJV1201 2.4 23.9 1.0 H481 A:ZJV1201 2.7 28.7 1.0 C49 A:ZJV1201 2.8 28.5 1.0 H492 A:ZJV1201 3.4 34.2 1.0 H493 A:ZJV1201 3.5 34.2 1.0 O42 A:ZJV1201 3.5 19.7 1.0 C41 A:ZJV1201 4.5 17.4 1.0 O43 A:ZJV1201 4.7 18.8 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-23 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1201 b:32.0 occ:1.00 F53 A:ZJV1201 0.0 32.0 1.0 C50 A:ZJV1201 1.4 29.5 1.0 F51 A:ZJV1201 2.2 34.2 1.0 F52 A:ZJV1201 2.2 38.2 1.0 C48 A:ZJV1201 2.4 23.9 1.0 O42 A:ZJV1201 2.7 19.7 1.0 H492 A:ZJV1201 2.9 34.2 1.0 C49 A:ZJV1201 3.0 28.5 1.0 H491 A:ZJV1201 3.0 34.2 1.0 H481 A:ZJV1201 3.2 28.7 1.0 HG22 A:VAL1158 3.4 33.7 1.0 HG13 A:VAL1158 3.8 37.0 1.0 C41 A:ZJV1201 3.8 17.4 1.0 H493 A:ZJV1201 3.9 34.2 1.0 HA A:VAL1158 4.3 28.0 1.0 CG2 A:VAL1158 4.3 28.1 1.0 O A:HOH1399 4.4 31.9 1.0 H401 A:ZJV1201 4.4 18.8 1.0 O43 A:ZJV1201 4.5 18.8 1.0 HG21 A:VAL1158 4.6 33.7 1.0 CG1 A:VAL1158 4.6 30.8 1.0 N40 A:ZJV1201 4.6 15.6 1.0 HG11 A:VAL1158 4.8 37.0 1.0 CB A:VAL1158 4.9 24.7 1.0 HG23 A:VAL1158 4.9 33.7 1.0

J.Zephyr, D.Nageswara Rao, S.V.Vo, M.Henes, K.Kosovrasti, A.N.Matthew, A.K.Hedger, J.Timm, E.T.Chan, A.Ali, N.Kurt Yilmaz, C.A.Schiffer. Deciphering the Molecular Mechanism of Hcv Protease Inhibitor Fluorination As A General Approach to Avoid Drug Resistance. J.Mol.Biol. V. 434 67503 2022.
ISSN: ESSN 1089-8638
PubMed: 35183560
DOI: 10.1016/J.JMB.2022.167503