Zinc in PDB 2hrv: 2A Cysteine Proteinase From Human Rhinovirus 2

All present enzymatic activity of 2A Cysteine Proteinase From Human Rhinovirus 2:
3.4.22.29;

The structure of 2A Cysteine Proteinase From Human Rhinovirus 2, PDB code: 2hrv was solved by J.F.W.Petersen, M.M.Cherney, H.-D.Liebig, T.Skern, E.Kuechler, M.N.G.James, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.95
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.921, 72.921, 161.659, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 25

The binding sites of Zinc atom in the 2A Cysteine Proteinase From Human Rhinovirus 2 (pdb code 2hrv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the 2A Cysteine Proteinase From Human Rhinovirus 2, PDB code: 2hrv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the 2A Cysteine Proteinase From Human Rhinovirus 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 2A Cysteine Proteinase From Human Rhinovirus 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn143 b:33.1 occ:1.00 ND1 A:HIS114 1.9 27.7 1.0 SG A:CYS52 2.3 34.1 1.0 SG A:CYS54 2.3 30.7 1.0 SG A:CYS112 2.4 26.3 1.0 CE1 A:HIS114 2.7 28.4 1.0 CG A:HIS114 3.1 28.4 1.0 CB A:CYS54 3.2 29.4 1.0 CB A:CYS52 3.2 36.4 1.0 CB A:CYS112 3.3 23.1 1.0 CB A:HIS114 3.6 26.6 1.0 NE2 A:HIS114 3.9 29.5 1.0 N A:HIS114 4.0 27.4 1.0 CD2 A:HIS114 4.1 28.2 1.0 N A:CYS54 4.2 33.7 1.0 CA A:CYS54 4.3 30.7 1.0 CA A:HIS114 4.4 27.2 1.0 CG A:PRO50 4.4 28.1 1.0 N A:LYS113 4.5 26.6 1.0 CA A:CYS52 4.6 35.8 1.0 CA A:CYS112 4.6 24.1 1.0 CG A:LYS113 4.7 30.4 1.0 C A:CYS112 4.8 25.2 1.0 CB A:PRO50 4.9 29.4 1.0 N A:ASP53 5.0 35.7 1.0 C A:CYS52 5.0 35.7 1.0 CG2 A:ILE117 5.0 20.2 1.0

Zinc binding site 2 out of 2 in the 2A Cysteine Proteinase From Human Rhinovirus 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 2A Cysteine Proteinase From Human Rhinovirus 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn143 b:30.9 occ:1.00 ND1 B:HIS114 2.1 26.7 1.0 SG B:CYS54 2.3 30.4 1.0 SG B:CYS52 2.3 28.9 1.0 SG B:CYS112 2.4 26.9 1.0 CE1 B:HIS114 2.9 27.9 1.0 CB B:CYS52 3.1 31.2 1.0 CG B:HIS114 3.2 27.8 1.0 CB B:CYS54 3.2 31.4 1.0 CB B:CYS112 3.3 24.5 1.0 CB B:HIS114 3.6 26.9 1.0 N B:HIS114 3.9 26.5 1.0 NE2 B:HIS114 4.1 28.3 1.0 CD2 B:HIS114 4.2 27.4 1.0 N B:CYS54 4.2 33.2 1.0 CA B:CYS54 4.3 31.4 1.0 CA B:HIS114 4.4 26.3 1.0 N B:LYS113 4.5 25.8 1.0 CA B:CYS52 4.5 32.2 1.0 CG B:PRO50 4.5 26.2 1.0 CA B:CYS112 4.6 24.1 1.0 CG B:LYS113 4.7 32.0 1.0 C B:CYS112 4.7 24.9 1.0 O B:HOH249 4.8 52.9 1.0 CB B:PRO50 4.8 27.4 1.0 CG2 B:ILE117 4.9 20.1 1.0 C B:CYS52 4.9 32.6 1.0 N B:ASP53 5.0 34.0 1.0 C B:LYS113 5.0 26.8 1.0

J.F.Petersen, M.M.Cherney, H.D.Liebig, T.Skern, E.Kuechler, M.N.James. The Structure of the 2A Proteinase From A Common Cold Virus: A Proteinase Responsible For the Shut-Off of Host-Cell Protein Synthesis. Embo J. V. 18 5463 1999.
ISSN: ISSN 0261-4189
PubMed: 10523291
DOI: 10.1093/EMBOJ/18.20.5463