Zinc in PDB 7mmk: Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 149

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 149, PDB code: 7mmk 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)	23.87 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.365, 58.604, 59.629, 90, 90, 90
R / Rfree (%)	16.2 / 20.8

The structure of Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 149 also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 149 (pdb code 7mmk). 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- 149, PDB code: 7mmk:

Zinc binding site 1 out of 1 in the Crystal Structure of Hcv NS3/4A D168A Protease in Complex with NR01- 149


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- 149 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1201 b:21.0 occ:1.00 ND1 A:HIS1149 2.1 22.4 1.0 SG A:CYS1097 2.3 16.4 1.0 SG A:CYS1145 2.3 14.5 1.0 SG A:CYS1099 2.3 20.5 1.0 HB2 A:HIS1149 2.8 15.3 1.0 HB2 A:CYS1099 2.8 21.2 1.0 CE1 A:HIS1149 3.1 22.7 1.0 CG A:HIS1149 3.1 18.1 1.0 H A:CYS1099 3.1 21.1 1.0 CB A:CYS1099 3.1 17.6 1.0 HB3 A:CYS1145 3.2 17.1 1.0 CB A:CYS1145 3.3 14.2 1.0 HE1 A:HIS1149 3.3 27.2 1.0 HA A:CYS1097 3.3 21.1 1.0 HB2 A:CYS1097 3.3 25.4 1.0 CB A:CYS1097 3.3 21.1 1.0 HB2 A:CYS1145 3.4 17.1 1.0 CB A:HIS1149 3.4 12.8 1.0 HB3 A:ALA1147 3.5 23.7 1.0 CA A:CYS1097 3.8 17.6 1.0 N A:CYS1099 3.8 17.5 1.0 H A:THR1098 3.8 19.3 1.0 HB3 A:CYS1099 3.9 21.2 1.0 H A:HIS1149 3.9 17.1 1.0 HB3 A:HIS1149 4.0 15.3 1.0 CA A:CYS1099 4.1 18.7 1.0 HB3 A:CYS1097 4.2 25.4 1.0 NE2 A:HIS1149 4.2 21.5 1.0 H A:ALA1147 4.2 17.8 1.0 CD2 A:HIS1149 4.2 22.9 1.0 N A:THR1098 4.3 16.1 1.0 O A:HOH1364 4.4 27.4 1.0 CB A:ALA1147 4.5 19.8 1.0 C A:CYS1097 4.5 18.3 1.0 CA A:HIS1149 4.6 16.4 1.0 N A:HIS1149 4.6 14.2 1.0 HA A:CYS1099 4.6 22.5 1.0 HB2 A:ALA1147 4.7 23.7 1.0 CA A:CYS1145 4.7 14.6 1.0 H A:CYS1145 4.7 14.6 1.0 HD2 A:PRO1146 4.7 15.7 1.0 HG22 A:VAL1151 4.8 20.4 1.0 C A:THR1098 4.9 20.3 1.0 HE2 A:HIS1149 5.0 25.9 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