Zinc in PDB 7t28: Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State

The structure of Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State, PDB code: 7t28 was solved by S.J.Hobbs, T.Wein, A.Lu, B.R.Morehouse, J.Schnabel, R.Sorek, P.J.Kranzusch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.26 / 2.68
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	82.485, 82.485, 76.098, 90, 90, 120
R / Rfree (%)	30 / 32

The binding sites of Zinc atom in the Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State (pdb code 7t28). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State, PDB code: 7t28:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:141.3 occ:1.00 CE1 A:HIS65 1.8 111.8 1.0 NE2 A:HIS156 2.3 117.4 1.0 NE2 A:HIS65 2.3 115.0 1.0 O A:HOH431 2.4 50.0 1.0 CD2 A:HIS156 2.6 99.7 1.0 ND1 A:HIS65 3.0 88.3 1.0 CE1 A:HIS156 3.3 116.6 1.0 CD2 A:HIS65 3.6 106.7 1.0 CG A:HIS156 3.7 100.1 1.0 ZN A:ZN302 3.9 93.8 1.0 CG A:HIS65 3.9 97.3 1.0 CE1 A:HIS209 4.0 104.5 1.0 ND1 A:HIS156 4.0 97.3 1.0 O A:HOH411 4.0 50.0 1.0 CE1 A:HIS231 4.0 108.0 1.0 NE2 A:HIS231 4.6 119.5 1.0 N A:THR181 4.7 79.3 1.0 CE1 A:HIS70 4.7 76.3 1.0 OD2 A:ASP69 4.8 82.6 1.0 NE2 A:HIS209 4.8 107.7 1.0 CB A:HIS156 4.9 103.0 1.0 ND1 A:HIS209 4.9 99.1 1.0 ND1 A:HIS231 4.9 107.4 1.0

Zinc binding site 2 out of 2 in the Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Phage BSP38 Anti-Pycsar Nuclease APYC1 in Apo State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:93.8 occ:1.00 NE2 A:HIS70 2.3 81.2 1.0 NE2 A:HIS231 2.3 119.5 1.0 CE1 A:HIS70 2.6 76.3 1.0 CE1 A:HIS231 2.8 108.0 1.0 O A:HOH431 2.8 50.0 1.0 CD2 A:HIS231 2.9 101.2 1.0 ND1 A:HIS231 3.5 107.4 1.0 CG A:HIS231 3.5 90.0 1.0 CD2 A:HIS70 3.6 81.8 1.0 ND1 A:HIS70 3.9 71.9 1.0 ZN A:ZN301 3.9 141.3 1.0 OD2 A:ASP69 4.0 82.6 1.0 CE1 A:HIS65 4.0 111.8 1.0 ND1 A:HIS65 4.1 88.3 1.0 O A:HOH411 4.1 50.0 1.0 C A:SER179 4.3 86.0 1.0 CG A:HIS70 4.3 76.2 1.0 OG A:SER179 4.5 70.2 1.0 CB A:ASN24 4.6 74.7 1.0 CB A:HIS231 4.8 90.1 1.0 O A:ASN24 4.8 80.8 1.0 ND2 A:ASN24 5.0 78.6 1.0 O A:SER179 5.0 98.6 1.0

S.J.Hobbs, T.Wein, A.Lu, B.R.Morehouse, J.Schnabel, A.Leavitt, E.Yirmiya, R.Sorek, P.J.Kranzusch. Phage Anti-Cbass and Anti-Pycsar Nucleases Subvert Bacterial Immunity. Nature V. 605 522 2022.
ISSN: ESSN 1476-4687
PubMed: 35395152
DOI: 10.1038/S41586-022-04716-Y