Zinc in PDB 7xmw: Crystal Structure of Anti-Crispr Protein ACRVIA2

The structure of Crystal Structure of Anti-Crispr Protein ACRVIA2, PDB code: 7xmw was solved by X.Yan, X.Li, G.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.13 / 2.59
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	123.377, 123.377, 123.377, 90, 90, 90
R / Rfree (%)	25.2 / 30.7

The binding sites of Zinc atom in the Crystal Structure of Anti-Crispr Protein ACRVIA2 (pdb code 7xmw). 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 Anti-Crispr Protein ACRVIA2, PDB code: 7xmw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Anti-Crispr Protein ACRVIA2


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 Anti-Crispr Protein ACRVIA2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:73.9 occ:1.00 SG A:CYS46 2.2 72.4 1.0 SG A:CYS49 2.3 82.5 1.0 SG A:CYS7 2.3 78.6 1.0 SG A:CYS4 2.3 78.6 1.0 HB3 A:CYS7 2.5 99.9 1.0 HB3 A:CYS49 2.8 96.5 1.0 CB A:CYS7 2.9 83.2 1.0 HB3 A:CYS4 3.1 83.1 1.0 CB A:CYS4 3.1 69.2 1.0 CB A:CYS49 3.1 80.4 1.0 HB2 A:CYS4 3.2 83.1 1.0 H A:CYS7 3.2 98.9 1.0 H A:CYS49 3.3 101.5 1.0 HB3 A:CYS46 3.5 84.2 1.0 CB A:CYS46 3.5 70.2 1.0 N A:CYS7 3.6 82.4 1.0 HB2 A:CYS46 3.6 84.2 1.0 HB2 A:LYS6 3.7 96.5 1.0 HB2 A:CYS7 3.7 99.9 1.0 CA A:CYS7 3.8 79.2 1.0 HB3 A:ASN51 3.8 93.8 1.0 HB2 A:CYS49 3.9 96.5 1.0 N A:CYS49 3.9 84.5 1.0 HB3 A:CYS9 3.9 95.4 1.0 H A:CYS9 4.0 86.6 1.0 H A:ASN51 4.1 86.3 1.0 CA A:CYS49 4.1 85.7 1.0 HB2 A:ASN51 4.2 93.8 1.0 H A:LYS6 4.2 97.1 1.0 CB A:ASN51 4.5 78.1 1.0 C A:LYS6 4.5 96.9 1.0 C A:CYS7 4.5 79.4 1.0 H A:GLY8 4.5 102.5 1.0 CB A:LYS6 4.5 80.3 1.0 H A:LYS48 4.6 96.5 1.0 HA A:CYS7 4.6 95.1 1.0 H A:ASP50 4.6 93.9 1.0 CA A:CYS4 4.6 72.7 1.0 HB2 A:CYS9 4.7 95.4 1.0 CB A:CYS9 4.7 79.4 1.0 N A:GLY8 4.8 85.4 1.0 C A:CYS49 4.8 83.9 1.0 HB3 A:LYS6 4.8 96.5 1.0 HA A:CYS49 4.9 102.9 1.0 CB A:LYS48 4.9 72.6 1.0 N A:CYS9 4.9 72.1 1.0 CA A:LYS6 4.9 81.0 1.0 N A:LYS6 4.9 80.9 1.0 N A:ASN51 4.9 71.8 1.0 N A:ASP50 4.9 78.2 1.0 C A:LYS48 4.9 89.6 1.0 CA A:CYS46 5.0 88.4 1.0 HA A:CYS4 5.0 87.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Anti-Crispr Protein ACRVIA2


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 Anti-Crispr Protein ACRVIA2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn102 b:70.9 occ:1.00 HB2 B:CYS49 2.0 78.1 1.0 HB2 B:CYS7 2.1 77.8 1.0 SG B:CYS7 2.3 108.0 1.0 SG B:CYS46 2.3 65.0 1.0 SG B:CYS49 2.3 116.3 1.0 SG B:CYS4 2.3 72.9 1.0 H B:CYS49 2.6 110.9 1.0 CB B:CYS49 2.6 65.3 1.0 CB B:CYS7 2.6 65.1 1.0 H B:CYS7 2.7 101.0 1.0 HB3 B:CYS4 3.0 83.6 1.0 CB B:CYS4 3.1 69.6 1.0 HB2 B:CYS4 3.1 83.6 1.0 CB B:CYS46 3.2 76.3 1.0 HB3 B:CYS46 3.2 91.6 1.0 HB2 B:CYS46 3.2 91.6 1.0 N B:CYS49 3.3 92.4 1.0 N B:CYS7 3.3 84.1 1.0 HB3 B:CYS49 3.3 78.1 1.0 HB3 B:CYS7 3.4 77.8 1.0 CA B:CYS49 3.5 85.3 1.0 CA B:CYS7 3.5 89.6 1.0 HB3 B:CYS9 3.8 90.0 1.0 HB2 B:LYS6 3.8 80.9 1.0 H B:CYS9 4.0 81.8 1.0 HA B:CYS49 4.0 102.5 1.0 HA B:CYS7 4.0 107.5 1.0 HB3 B:ASN51 4.0 90.7 1.0 H B:LYS48 4.1 93.5 1.0 HB2 B:ASN51 4.2 90.7 1.0 H B:ASN51 4.2 84.7 1.0 H B:LYS6 4.3 87.8 1.0 HB2 B:CYS9 4.4 90.0 1.0 H B:ASP50 4.4 77.7 1.0 C B:LYS6 4.5 87.0 1.0 CB B:CYS9 4.5 75.0 1.0 C B:LYS48 4.5 77.8 1.0 H B:GLY8 4.5 78.8 1.0 CA B:CYS4 4.6 70.7 1.0 CB B:ASN51 4.6 75.5 1.0 CA B:CYS46 4.6 72.1 1.0 C B:CYS7 4.7 65.3 1.0 CB B:LYS6 4.7 67.4 1.0 C B:CYS49 4.7 77.5 1.0 CB B:LYS48 4.7 69.8 1.0 N B:CYS9 4.8 68.1 1.0 N B:GLY8 4.8 65.6 1.0 N B:ASP50 4.8 65.0 1.0 N B:LYS48 4.9 77.9 1.0 HA B:CYS4 4.9 85.0 1.0 HA B:CYS46 4.9 86.6 1.0 N B:LYS6 5.0 73.1 1.0 CA B:LYS6 5.0 76.4 1.0 HD22 B:ASN51 5.0 93.8 1.0 CA B:LYS48 5.0 74.7 1.0 N B:ASN51 5.0 70.6 1.0 HB3 B:LYS6 5.0 80.9 1.0

G.Song, X.Li, Z.Wang, C.Dong, X.Xie, X.Yan. Structure of ACRVIA2 and Its Binding Mechanism to Crispr-CAS13A. Biochem.Biophys.Res.Commun. V. 612 84 2022.
ISSN: ESSN 1090-2104
PubMed: 35512461
DOI: 10.1016/J.BBRC.2022.04.091