Zinc in PDB 7mmg: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58

All present enzymatic activity of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58:
3.4.21.98;

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58, PDB code: 7mmg 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)	42.51 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.854, 50.987, 77.068, 90, 92.84, 90
R / Rfree (%)	19.9 / 24.8

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58 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 NR02-58 (pdb code 7mmg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58, PDB code: 7mmg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58


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 NR02-58 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1203 b:35.7 occ:1.00 SG A:CYS1099 2.3 58.0 1.0 SG A:CYS1097 2.3 27.0 1.0 SG A:CYS1145 2.3 23.9 1.0 HB2 A:CYS1099 2.3 40.7 1.0 ND1 A:HIS1149 2.7 33.8 1.0 CB A:CYS1099 2.8 33.8 1.0 H A:CYS1099 2.9 46.2 1.0 HB2 A:HIS1149 3.0 23.7 1.0 HB2 A:CYS1097 3.1 29.0 1.0 HB3 A:CYS1145 3.2 32.4 1.0 CB A:CYS1145 3.2 26.9 1.0 CB A:CYS1097 3.2 24.1 1.0 HB2 A:CYS1145 3.3 32.4 1.0 HA A:CYS1097 3.4 32.4 1.0 N A:CYS1099 3.5 38.4 1.0 CG A:HIS1149 3.5 27.9 1.0 H A:THR1098 3.5 36.7 1.0 HB3 A:CYS1099 3.5 40.7 1.0 HB3 A:ALA1147 3.6 43.8 1.0 CE1 A:HIS1149 3.6 31.2 1.0 CB A:HIS1149 3.7 19.7 1.0 CA A:CYS1099 3.7 34.3 1.0 CA A:CYS1097 3.8 26.9 1.0 HE1 A:HIS1149 3.8 37.6 1.0 N A:THR1098 4.0 30.5 1.0 H A:HIS1149 4.0 25.9 1.0 HB3 A:CYS1097 4.1 29.0 1.0 HB3 A:HIS1149 4.2 23.7 1.0 HA A:CYS1099 4.2 41.3 1.0 H A:ALA1147 4.3 36.5 1.0 C A:CYS1097 4.3 31.7 1.0 CB A:ALA1147 4.5 36.4 1.0 C A:THR1098 4.5 39.3 1.0 HD2 A:PRO1146 4.5 26.6 1.0 CA A:CYS1145 4.6 22.4 1.0 CD2 A:HIS1149 4.7 29.6 1.0 HB2 A:ALA1147 4.7 43.8 1.0 NE2 A:HIS1149 4.7 28.5 1.0 H A:CYS1145 4.7 22.4 1.0 N A:HIS1149 4.7 21.5 1.0 CA A:HIS1149 4.8 21.5 1.0 O A:HOH1301 4.8 28.7 1.0 H A:SER1101 4.9 37.0 1.0 H A:GLY1100 4.9 47.7 1.0 HG A:SER1101 4.9 44.0 1.0 CA A:THR1098 4.9 37.6 1.0 C A:CYS1099 4.9 39.4 1.0 HB3 A:SER1101 5.0 32.9 1.0 HG22 A:VAL1151 5.0 29.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR02-58 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1302 b:22.7 occ:1.00 SG B:CYS1099 2.3 54.7 1.0 ND1 B:HIS1149 2.3 31.1 1.0 SG B:CYS1097 2.3 18.8 1.0 SG B:CYS1145 2.4 15.9 1.0 HB2 B:CYS1099 2.5 35.4 1.0 HB2 B:HIS1149 2.9 22.1 1.0 H B:CYS1099 2.9 32.2 1.0 CB B:CYS1099 2.9 29.4 1.0 HB2 B:CYS1097 3.0 28.8 1.0 HB3 B:CYS1145 3.1 18.5 1.0 CB B:CYS1097 3.2 23.9 1.0 CB B:CYS1145 3.2 15.4 1.0 HB2 B:CYS1145 3.3 18.5 1.0 CG B:HIS1149 3.3 20.8 1.0 CE1 B:HIS1149 3.3 27.4 1.0 HA B:CYS1097 3.3 21.2 1.0 HE1 B:HIS1149 3.5 33.0 1.0 CB B:HIS1149 3.5 18.4 1.0 N B:CYS1099 3.6 26.7 1.0 HB3 B:CYS1099 3.6 35.4 1.0 HB3 B:ALA1147 3.8 27.9 1.0 CA B:CYS1097 3.8 17.6 1.0 CA B:CYS1099 3.9 26.0 1.0 HB3 B:HIS1149 4.0 22.1 1.0 H B:THR1098 4.0 34.3 1.0 HB3 B:CYS1097 4.0 28.8 1.0 H B:HIS1149 4.2 16.7 1.0 N B:THR1098 4.3 28.5 1.0 H B:ALA1147 4.4 26.3 1.0 NE2 B:HIS1149 4.4 25.7 1.0 CD2 B:HIS1149 4.4 22.1 1.0 C B:CYS1097 4.4 26.3 1.0 HA B:CYS1099 4.5 31.3 1.0 HB3 B:SER1101 4.6 36.5 1.0 H B:SER1101 4.6 31.4 1.0 H B:GLY1100 4.6 36.3 1.0 CB B:ALA1147 4.7 23.1 1.0 CA B:CYS1145 4.7 16.3 1.0 HD2 B:PRO1146 4.7 23.8 1.0 HG23 B:VAL1151 4.7 26.4 1.0 CA B:HIS1149 4.7 15.3 1.0 HB2 B:ALA1147 4.8 27.9 1.0 H B:CYS1145 4.8 22.9 1.0 C B:THR1098 4.8 29.3 1.0 N B:HIS1149 4.9 14.3 1.0 C B:CYS1099 4.9 29.3 1.0 N B:GLY1100 5.0 30.2 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