Zinc in PDB 7l7l: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129, PDB code: 7l7l 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)	20.99 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.856, 58.773, 59.98, 90, 90, 90
R / Rfree (%)	16.6 / 20.8

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129 also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Zinc atom in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129 (pdb code 7l7l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129, PDB code: 7l7l:

Zinc binding site 1 out of 1 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 129 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1201 b:22.9 occ:1.00 ND1 A:HIS1149 2.1 26.6 1.0 SG A:CYS1097 2.3 20.3 1.0 SG A:CYS1145 2.3 19.3 1.0 SG A:CYS1099 2.3 22.1 1.0 HB2 A:HIS1149 2.8 28.1 1.0 HB2 A:CYS1099 2.9 27.6 1.0 CE1 A:HIS1149 3.0 31.9 1.0 CG A:HIS1149 3.1 24.6 1.0 H A:CYS1099 3.2 26.1 1.0 HE1 A:HIS1149 3.2 38.4 1.0 CB A:CYS1099 3.2 23.0 1.0 HB3 A:CYS1145 3.2 25.2 1.0 CB A:CYS1145 3.3 21.0 1.0 HA A:CYS1097 3.4 22.9 1.0 CB A:HIS1149 3.4 23.4 1.0 CB A:CYS1097 3.4 20.3 1.0 HB2 A:CYS1097 3.4 24.3 1.0 HB2 A:CYS1145 3.5 25.2 1.0 HB3 A:ALA1147 3.7 24.7 1.0 H A:THR1098 3.8 25.4 1.0 H A:HIS1149 3.9 25.6 1.0 CA A:CYS1097 3.9 19.1 1.0 N A:CYS1099 3.9 21.7 1.0 HB3 A:CYS1099 3.9 27.6 1.0 HO2 A:EDO1203 3.9 42.2 1.0 HB3 A:HIS1149 4.0 28.1 1.0 NE2 A:HIS1149 4.1 29.3 1.0 CA A:CYS1099 4.2 22.7 1.0 CD2 A:HIS1149 4.2 28.3 1.0 HB3 A:CYS1097 4.2 24.3 1.0 O A:HOH1379 4.3 31.2 1.0 N A:THR1098 4.3 21.1 1.0 H A:ALA1147 4.3 23.7 1.0 CA A:HIS1149 4.5 22.5 1.0 N A:HIS1149 4.5 21.4 1.0 C A:CYS1097 4.5 22.9 1.0 CB A:ALA1147 4.6 20.6 1.0 HA A:CYS1099 4.7 27.2 1.0 HD2 A:PRO1146 4.7 23.7 1.0 H A:CYS1145 4.7 22.9 1.0 CA A:CYS1145 4.8 19.5 1.0 O2 A:EDO1203 4.8 35.1 1.0 HG22 A:VAL1151 4.8 24.8 1.0 HE2 A:HIS1149 4.9 35.2 1.0 HB2 A:ALA1147 4.9 24.7 1.0 C A:THR1098 5.0 27.9 1.0

D.Nageswara Rao, J.Zephyr, M.Henes, E.T.Chan, A.N.Matthew, A.K.Hedger, H.L.Conway, M.Saeed, A.Newton, C.J.Petropoulos, W.Huang, N.Kurt Yilmaz, C.A.Schiffer, A.Ali. Discovery of Quinoxaline-Based P1-P3 Macrocyclic NS3/4A Protease Inhibitors with Potent Activity Against Drug-Resistant Hepatitis C Virus Variants. J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
PubMed: 34405680
DOI: 10.1021/ACS.JMEDCHEM.1C00554