Fluorine in PDB 7mmj: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-08

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-08, PDB code: 7mmj 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)	25.10 / 1.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.328, 58.941, 95.756, 90, 90, 90
R / Rfree (%)	19.5 / 23.9

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-08 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 NR02-08 (pdb code 7mmj). 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 Hcv NS3/4A D168A Protease in Complex with NR02-08, PDB code: 7mmj:

Fluorine binding site 1 out of 1 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-08


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 NR02-08 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1202 b:37.2 occ:1.00 F55 A:ZJM1202 0.0 37.2 1.0 C51 A:ZJM1202 1.4 36.5 1.0 H511 A:ZJM1202 2.0 44.1 1.0 H501 A:ZJM1202 2.1 49.0 1.0 C50 A:ZJM1202 2.2 40.6 1.0 C52 A:ZJM1202 2.5 34.4 1.0 H521 A:ZJM1202 2.5 41.5 1.0 HB3 A:ALA1156 2.9 27.5 1.0 H522 A:ZJM1202 3.0 41.5 1.0 O20 A:ZJM1202 3.2 35.7 1.0 CB A:ALA1168 3.4 26.1 1.0 C54 A:ZJM1202 3.5 39.1 1.0 C53 A:ZJM1202 3.6 43.5 1.0 CB A:ALA1156 3.6 22.6 1.0 HB1 A:ALA1156 3.7 27.5 1.0 H542 A:ZJM1202 3.7 47.2 1.0 HH21 A:ARG1155 3.8 40.5 0.5 HB2 A:ALA1156 4.0 27.5 1.0 NH2 A:ARG1155 4.1 33.5 0.5 HE A:ARG1123 4.2 32.1 1.0 HH21 A:ARG1123 4.2 38.9 1.0 H531 A:ZJM1202 4.2 52.4 1.0 C19 A:ZJM1202 4.3 34.6 1.0 H532 A:ZJM1202 4.3 52.4 1.0 H541 A:ZJM1202 4.3 47.2 1.0 O A:HOH1352 4.3 40.9 1.0 NE A:ARG1123 4.3 26.5 1.0 NH2 A:ARG1123 4.3 32.2 1.0 HH22 A:ARG1155 4.3 40.5 0.5 H321 A:ZJM1202 4.3 37.6 1.0 CZ A:ARG1123 4.3 39.0 1.0 H322 A:ZJM1202 4.4 37.6 1.0 H323 A:ZJM1202 4.4 37.6 1.0 HG23 A:VAL1158 4.5 37.0 1.0 O21 A:ZJM1202 4.5 27.2 1.0 C32 A:ZJM1202 4.6 31.1 1.0 HH22 A:ARG1123 4.7 38.9 1.0 HE A:ARG1155 4.7 37.8 0.5 CA A:ALA1168 4.8 22.6 1.0 CZ A:ARG1155 4.8 33.4 0.5 HD2 A:ARG1123 4.8 46.2 1.0 HG2 A:ARG1155 4.9 30.7 0.5 HG21 A:VAL1158 4.9 37.0 1.0 CA A:ALA1156 4.9 23.6 1.0 HD3 A:ARG1123 4.9 46.2 1.0 H A:ALA1168 5.0 29.0 1.0 CD A:ARG1123 5.0 38.3 1.0 NH1 A:ARG1123 5.0 33.8 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