Zinc in PDB 8z3r: The Structure of Type III Crispr-Associated Deaminase in Complex CA4

The binding sites of Zinc atom in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4 (pdb code 8z3r). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4, PDB code: 8z3r:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:99.3 occ:1.00 NE2 A:HIS266 2.3 49.6 1.0 NE2 A:HIS264 2.3 46.1 1.0 NE2 A:HIS471 2.3 55.7 1.0 CE1 A:HIS471 2.7 49.3 1.0 OD1 A:ASP569 3.0 65.5 1.0 CE1 A:HIS266 3.1 44.9 1.0 CE1 A:HIS264 3.1 44.3 1.0 CD2 A:HIS264 3.4 45.0 1.0 CD2 A:HIS266 3.4 51.8 1.0 CD2 A:HIS471 3.6 48.9 1.0 ND1 A:HIS471 4.0 47.6 1.0 CG A:ASP569 4.1 59.8 1.0 NH1 A:ARG354 4.2 48.3 1.0 ND1 A:HIS266 4.3 48.7 1.0 ND1 A:HIS264 4.3 45.4 1.0 CE1 A:HIS495 4.4 49.3 1.0 CG A:HIS471 4.4 43.1 1.0 OD2 A:ASP569 4.4 61.6 1.0 CG A:HIS266 4.5 49.1 1.0 CG A:HIS264 4.5 41.5 1.0 ND1 A:HIS495 5.0 45.6 1.0

Zinc binding site 2 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:110.3 occ:1.00 CE1 B:HIS471 2.1 57.5 1.0 NE2 B:HIS264 2.3 51.6 1.0 NE2 B:HIS266 2.3 49.4 1.0 NE2 B:HIS471 2.3 55.9 1.0 CE1 B:HIS266 2.9 43.2 1.0 CE1 B:HIS264 3.0 48.0 1.0 ND1 B:HIS471 3.4 52.4 1.0 CD2 B:HIS264 3.5 47.3 1.0 CD2 B:HIS266 3.5 50.4 1.0 CD2 B:HIS471 3.7 51.5 1.0 OD1 B:ASP569 4.0 62.6 1.0 CG B:HIS471 4.2 46.9 1.0 ND1 B:HIS266 4.2 47.2 1.0 ND1 B:HIS264 4.2 47.0 1.0 CG B:HIS264 4.5 42.8 1.0 CG B:HIS266 4.5 46.6 1.0 NE2 B:HIS495 4.7 53.0 1.0 NH1 B:ARG354 4.8 54.4 1.0 CD2 B:HIS495 4.9 45.2 1.0 CG B:ASP569 4.9 62.8 1.0 OD1 B:ASP440 5.0 58.9 1.0

Zinc binding site 3 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn701 b:98.5 occ:1.00 NE2 C:HIS266 2.3 45.9 1.0 NE2 C:HIS264 2.3 45.3 1.0 NE2 C:HIS471 2.3 53.2 1.0 CE1 C:HIS471 3.0 47.2 1.0 OD1 C:ASP569 3.1 62.4 1.0 CE1 C:HIS264 3.2 42.6 1.0 CE1 C:HIS266 3.2 44.3 1.0 CD2 C:HIS266 3.4 44.7 1.0 CD2 C:HIS264 3.4 45.3 1.0 CD2 C:HIS471 3.5 45.5 1.0 CG C:ASP569 4.1 59.2 1.0 ND1 C:HIS471 4.2 49.3 1.0 ND1 C:HIS264 4.3 43.8 1.0 ND1 C:HIS266 4.3 49.8 1.0 OD2 C:ASP569 4.4 62.4 1.0 CG C:HIS471 4.5 42.3 1.0 CG C:HIS266 4.5 43.7 1.0 CG C:HIS264 4.5 42.9 1.0 NH1 C:ARG354 4.6 46.8 1.0 CE1 C:HIS495 4.9 51.8 1.0

Zinc binding site 4 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn701 b:99.9 occ:1.00 NE2 D:HIS264 2.3 50.0 1.0 NE2 D:HIS266 2.3 47.4 1.0 NE2 D:HIS471 2.3 54.9 1.0 CE1 D:HIS471 2.7 49.0 1.0 OD2 D:ASP569 3.1 60.4 1.0 CE1 D:HIS266 3.2 45.4 1.0 CE1 D:HIS264 3.2 46.4 1.0 CD2 D:HIS264 3.3 45.2 1.0 CD2 D:HIS266 3.4 49.9 1.0 CD2 D:HIS471 3.6 48.5 1.0 ND1 D:HIS471 4.0 48.7 1.0 CG D:ASP569 4.1 58.2 1.0 ND1 D:HIS264 4.3 46.8 1.0 CE1 D:HIS495 4.3 52.2 1.0 OD1 D:ASP569 4.3 60.8 1.0 ND1 D:HIS266 4.3 51.4 1.0 CG D:HIS264 4.4 40.5 1.0 NH1 D:ARG354 4.4 47.6 1.0 CG D:HIS471 4.4 45.0 1.0 CG D:HIS266 4.5 46.6 1.0 ND1 D:HIS495 4.9 49.4 1.0

Zinc binding site 5 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn701 b:109.1 occ:1.00 NE2 E:HIS471 2.3 52.7 1.0 NE2 E:HIS266 2.3 46.0 1.0 NE2 E:HIS264 2.3 50.3 1.0 CE1 E:HIS471 2.9 49.6 1.0 CE1 E:HIS264 3.0 45.7 1.0 OD1 E:ASP569 3.3 62.1 1.0 CD2 E:HIS266 3.3 45.3 1.0 CE1 E:HIS266 3.3 46.3 1.0 CD2 E:HIS264 3.5 48.9 1.0 CD2 E:HIS471 3.5 46.3 1.0 CG E:ASP569 4.1 57.6 1.0 ND1 E:HIS471 4.2 50.5 1.0 ND1 E:HIS264 4.2 44.6 1.0 CE1 E:HIS495 4.2 55.9 1.0 OD2 E:ASP569 4.3 63.3 1.0 ND1 E:HIS266 4.4 51.4 1.0 CG E:HIS266 4.4 44.2 1.0 CG E:HIS471 4.5 44.0 1.0 CG E:HIS264 4.5 43.7 1.0 NH1 E:ARG354 4.7 44.6 1.0 ND1 E:HIS495 4.8 51.0 1.0

Zinc binding site 6 out of 6 in the The Structure of Type III Crispr-Associated Deaminase in Complex CA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of The Structure of Type III Crispr-Associated Deaminase in Complex CA4 within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn701 b:105.3 occ:1.00 NE2 F:HIS264 2.3 49.1 1.0 NE2 F:HIS266 2.3 55.1 1.0 NE2 F:HIS471 2.3 58.7 1.0 CE1 F:HIS471 3.0 54.6 1.0 CE1 F:HIS264 3.0 47.1 1.0 CE1 F:HIS266 3.1 49.8 1.0 OD1 F:ASP569 3.3 60.1 1.0 CD2 F:HIS471 3.4 51.2 1.0 CD2 F:HIS266 3.4 55.1 1.0 CD2 F:HIS264 3.4 49.5 1.0 ND1 F:HIS471 4.2 55.1 1.0 CG F:ASP569 4.2 58.6 1.0 ND1 F:HIS264 4.3 46.5 1.0 CE1 F:HIS495 4.3 54.7 1.0 ND1 F:HIS266 4.3 54.5 1.0 CG F:HIS471 4.4 46.6 1.0 CG F:HIS264 4.5 43.6 1.0 CG F:HIS266 4.5 51.3 1.0 OD2 F:ASP569 4.6 63.9 1.0 NH1 F:ARG354 4.9 56.4 1.0 ND1 F:HIS495 4.9 49.5 1.0

Y.Li, Z.Li, P.Yan, C.Hua, J.Kong, W.Wu, Y.Cui, Y.Duan, S.Li, G.Li, S.Ji, Y.Chen, Y.Zhao, P.Yang, C.Hu, M.Lu, M.Chen, Y.Xiao. Antiviral Signaling of A Type III Crispr-Associated Deaminase. Science R0393 2024.
ISSN: ESSN 1095-9203
PubMed: 39666823
DOI: 10.1126/SCIENCE.ADR0393