Zinc in PDB 7ara: Rhinovirus A2 2A Protease in Complex with Zvam.Fmk

All present enzymatic activity of Rhinovirus A2 2A Protease in Complex with Zvam.Fmk:
2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15;

The structure of Rhinovirus A2 2A Protease in Complex with Zvam.Fmk, PDB code: 7ara was solved by K.M.Deutschmann-Olek, T.Skern, G.A.Bezerra, W.W.Yue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.00 / 2.24
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.647, 74.647, 160.831, 90, 90, 120
R / Rfree (%)	21.4 / 25.7

The binding sites of Zinc atom in the Rhinovirus A2 2A Protease in Complex with Zvam.Fmk (pdb code 7ara). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Rhinovirus A2 2A Protease in Complex with Zvam.Fmk, PDB code: 7ara:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Rhinovirus A2 2A Protease in Complex with Zvam.Fmk


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rhinovirus A2 2A Protease in Complex with Zvam.Fmk within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:65.3 occ:1.00 ND1 A:HIS114 2.1 49.0 1.0 SG A:CYS54 2.2 83.9 1.0 SG A:CYS52 2.4 76.3 1.0 SG A:CYS112 2.4 49.9 1.0 CE1 A:HIS114 2.7 39.1 1.0 CB A:CYS54 2.9 40.0 1.0 CG A:HIS114 3.3 50.9 1.0 CB A:CYS112 3.6 28.1 1.0 CB A:CYS52 3.7 60.1 1.0 N A:CYS54 3.7 68.0 1.0 CB A:HIS114 3.9 47.0 1.0 NE2 A:HIS114 3.9 47.6 1.0 CA A:CYS54 3.9 47.3 1.0 CD2 A:HIS114 4.2 38.5 1.0 N A:HIS114 4.3 36.3 1.0 N A:ASP53 4.4 65.6 1.0 N A:LYS113 4.5 40.0 1.0 CG A:PRO50 4.7 33.7 1.0 CA A:HIS114 4.8 38.3 1.0 C A:ASP53 4.9 72.1 1.0 CA A:CYS112 4.9 28.9 1.0 CA A:CYS52 5.0 66.3 1.0

Zinc binding site 2 out of 2 in the Rhinovirus A2 2A Protease in Complex with Zvam.Fmk


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Rhinovirus A2 2A Protease in Complex with Zvam.Fmk within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:56.6 occ:1.00 ND1 B:HIS114 2.0 54.3 1.0 SG B:CYS52 2.3 64.3 1.0 SG B:CYS112 2.3 51.3 1.0 SG B:CYS54 2.3 68.0 1.0 CE1 B:HIS114 2.7 42.5 1.0 CG B:HIS114 3.0 44.6 1.0 CB B:CYS54 3.1 35.0 1.0 CB B:CYS52 3.2 57.3 1.0 CB B:CYS112 3.5 36.9 1.0 CB B:HIS114 3.6 44.0 1.0 NE2 B:HIS114 3.8 41.9 1.0 CD2 B:HIS114 3.9 37.1 1.0 N B:CYS54 4.1 48.0 1.0 N B:HIS114 4.2 39.0 1.0 CA B:CYS54 4.3 43.4 1.0 CG B:PRO50 4.4 24.3 1.0 CA B:HIS114 4.5 32.2 1.0 N B:LYS113 4.6 29.3 1.0 CA B:CYS52 4.6 47.1 1.0 CG B:LYS113 4.7 53.7 1.0 CB B:PRO50 4.8 44.4 1.0 CA B:CYS112 4.8 41.4 1.0 CG2 B:ILE117 4.9 33.9 1.0 N B:ASP53 4.9 58.4 1.0 C B:CYS112 5.0 34.8 1.0

K.M.Deutschmann-Olek, W.W.Yue, G.A.Bezerra, T.Skern. Defining Substrate Selection By Rhinoviral 2A Proteinase Through Its Crystal Structure with the Inhibitor Zvam.Fmk Virology 2021.
ISSN: ISSN 0042-6822
DOI: 10.1016/J.VIROL.2021.07.008