Zinc in PDB 7mml: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 145

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 145, PDB code: 7mml 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)	27.02 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.037, 58.592, 59.565, 90, 90, 90
R / Rfree (%)	16 / 19.4

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 145 also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Zinc atom in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 145 (pdb code 7mml). 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- 145, PDB code: 7mml:

Zinc binding site 1 out of 1 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 145


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- 145 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1202 b:19.1 occ:1.00 ND1 A:HIS1149 2.3 23.8 1.0 SG A:CYS1099 2.3 20.0 1.0 SG A:CYS1145 2.3 13.5 1.0 SG A:CYS1097 2.3 15.2 1.0 HB2 A:CYS1099 2.7 19.0 1.0 HB2 A:HIS1149 2.9 16.6 1.0 CB A:CYS1099 3.1 15.8 1.0 H A:CYS1099 3.1 22.6 1.0 HB3 A:CYS1145 3.2 15.5 1.0 CB A:CYS1145 3.2 12.9 1.0 CG A:HIS1149 3.3 16.3 1.0 CE1 A:HIS1149 3.3 20.6 1.0 HA A:CYS1097 3.3 17.3 1.0 HB2 A:CYS1145 3.4 15.5 1.0 HE1 A:HIS1149 3.4 24.7 1.0 CB A:CYS1097 3.4 15.1 1.0 HB2 A:CYS1097 3.5 18.2 1.0 CB A:HIS1149 3.5 13.9 1.0 HB3 A:ALA1147 3.5 22.6 1.0 HB3 A:CYS1099 3.8 19.0 1.0 N A:CYS1099 3.8 18.8 1.0 CA A:CYS1097 3.8 14.4 1.0 H A:THR1098 3.8 18.3 1.0 H A:HIS1149 4.0 15.2 1.0 CA A:CYS1099 4.1 13.9 1.0 HB3 A:HIS1149 4.1 16.6 1.0 N A:THR1098 4.2 15.3 1.0 HB3 A:CYS1097 4.3 18.2 1.0 H A:ALA1147 4.3 16.3 1.0 O A:HOH1340 4.3 31.7 1.0 NE2 A:HIS1149 4.4 22.1 1.0 CD2 A:HIS1149 4.4 21.9 1.0 CB A:ALA1147 4.4 18.9 1.0 C A:CYS1097 4.5 14.8 1.0 HB2 A:ALA1147 4.5 22.6 1.0 HA A:CYS1099 4.6 16.7 1.0 HD2 A:PRO1146 4.6 16.8 1.0 CA A:HIS1149 4.7 14.2 1.0 CA A:CYS1145 4.7 11.7 1.0 N A:HIS1149 4.7 12.7 1.0 H A:CYS1145 4.8 15.2 1.0 HG22 A:VAL1151 4.8 15.2 1.0 C A:THR1098 4.9 19.0 1.0 O A:HOH1415 5.0 31.7 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