Magnesium in PDB 9c67: Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form

The binding sites of Magnesium atom in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form (pdb code 9c67). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form, PDB code: 9c67:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg701 b:146.4 occ:1.00 NE2 A:HIS243 2.1 159.8 1.0 OD1 A:ASP533 2.2 187.6 1.0 CE1 A:HIS245 2.2 159.6 1.0 CE1 A:HIS243 2.6 159.8 1.0 ND1 A:HIS245 3.0 159.6 1.0 CG A:ASP533 3.2 187.6 1.0 NE2 A:HIS245 3.2 159.6 1.0 CD2 A:HIS243 3.4 159.8 1.0 OD2 A:ASP533 3.5 187.6 1.0 ND1 A:HIS243 3.9 159.8 1.0 CG A:HIS245 4.2 159.6 1.0 CD2 A:HIS245 4.2 159.6 1.0 CG A:HIS243 4.3 159.8 1.0 CB A:ASP533 4.5 187.6 1.0 NE2 A:HIS472 4.7 178.2 1.0 CD2 A:HIS448 4.8 174.6 1.0 CA A:ASP533 4.8 187.6 1.0

Magnesium binding site 2 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:184.3 occ:1.00 OD1 B:ASP533 2.1 215.9 1.0 NE2 B:HIS245 2.1 188.7 1.0 NE2 B:HIS243 2.1 189.9 1.0 CE1 B:HIS243 2.8 189.9 1.0 CD2 B:HIS245 2.9 188.7 1.0 CE1 B:HIS245 3.2 188.7 1.0 CG B:ASP533 3.2 215.9 1.0 CD2 B:HIS243 3.3 189.9 1.0 OD2 B:ASP533 3.8 215.9 1.0 ND1 B:HIS243 4.1 189.9 1.0 CG B:HIS245 4.1 188.7 1.0 ND1 B:HIS245 4.2 188.7 1.0 CG B:HIS243 4.3 189.9 1.0 CB B:ASP533 4.3 215.9 1.0 ND2 B:ASN534 4.5 231.8 1.0 NH1 B:ARG333 4.5 181.2 1.0 CA B:ASP533 4.6 215.9 1.0

Magnesium binding site 3 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg701 b:142.3 occ:1.00 NE2 C:HIS243 2.1 159.7 1.0 CE1 C:HIS245 2.3 161.6 1.0 OD1 C:ASP533 2.4 185.2 1.0 CE1 C:HIS243 2.7 159.7 1.0 NE2 C:HIS245 3.1 161.6 1.0 ND1 C:HIS245 3.2 161.6 1.0 CG C:ASP533 3.2 185.2 1.0 CD2 C:HIS243 3.4 159.7 1.0 OD2 C:ASP533 3.5 185.2 1.0 ND1 C:HIS243 3.9 159.7 1.0 CD2 C:HIS245 4.3 161.6 1.0 CG C:HIS243 4.3 159.7 1.0 CG C:HIS245 4.3 161.6 1.0 CB C:ASP533 4.5 185.2 1.0 NE2 C:HIS472 4.6 178.7 1.0 CA C:ASP533 5.0 185.2 1.0

Magnesium binding site 4 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg701 b:174.3 occ:1.00 OD1 D:ASP533 2.1 211.3 1.0 NE2 D:HIS243 2.1 188.1 1.0 NE2 D:HIS245 2.1 188.6 1.0 CE1 D:HIS243 2.4 188.1 1.0 CD2 D:HIS245 3.0 188.6 1.0 CE1 D:HIS245 3.1 188.6 1.0 CG D:ASP533 3.1 211.3 1.0 CD2 D:HIS243 3.5 188.1 1.0 ND1 D:HIS243 3.7 188.1 1.0 OD2 D:ASP533 3.7 211.3 1.0 CB D:ASP533 4.1 211.3 1.0 CG D:HIS245 4.1 188.6 1.0 ND1 D:HIS245 4.1 188.6 1.0 CA D:ASP533 4.2 211.3 1.0 CG D:HIS243 4.2 188.1 1.0 C D:ASP533 4.5 211.3 1.0 NH1 D:ARG333 4.6 176.9 1.0 O D:ASP533 4.7 211.3 1.0

Magnesium binding site 5 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg701 b:148.4 occ:1.00 OD1 E:ASP533 2.1 181.7 1.0 NE2 E:HIS243 2.1 158.1 1.0 CE1 E:HIS245 2.2 158.8 1.0 CE1 E:HIS243 2.9 158.1 1.0 NE2 E:HIS245 3.1 158.8 1.0 ND1 E:HIS245 3.1 158.8 1.0 CG E:ASP533 3.2 181.7 1.0 CD2 E:HIS243 3.3 158.1 1.0 OD2 E:ASP533 3.6 181.7 1.0 ND1 E:HIS243 4.1 158.1 1.0 CD2 E:HIS245 4.2 158.8 1.0 CG E:HIS245 4.2 158.8 1.0 CG E:HIS243 4.3 158.1 1.0 CB E:ASP533 4.4 181.7 1.0 CE1 E:HIS472 4.6 184.4 1.0 CA E:ASP533 4.7 181.7 1.0

Magnesium binding site 6 out of 6 in the Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Cryoem Structure of Crispr Associated Effector, Carf-Adenosine Deaminase 1, CAD1, in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg701 b:194.5 occ:1.00 OD1 F:ASP533 2.0 217.9 1.0 NE2 F:HIS243 2.1 194.9 1.0 NE2 F:HIS245 2.1 199.7 1.0 CE1 F:HIS243 2.6 194.9 1.0 CD2 F:HIS245 2.9 199.7 1.0 CG F:ASP533 3.1 217.9 1.0 CE1 F:HIS245 3.3 199.7 1.0 CD2 F:HIS243 3.4 194.9 1.0 NH2 F:ARG333 3.4 188.9 1.0 OD2 F:ASP533 3.7 217.9 1.0 ND1 F:HIS243 3.9 194.9 1.0 CG F:HIS245 4.1 199.7 1.0 ND1 F:HIS245 4.3 199.7 1.0 CB F:ASP533 4.3 217.9 1.0 CG F:HIS243 4.3 194.9 1.0 ND2 F:ASN534 4.3 230.5 1.0 CZ F:ARG333 4.4 188.9 1.0 CA F:ASP533 4.6 217.9 1.0 NH1 F:ARG333 4.9 188.9 1.0 C F:ASP533 5.0 217.9 1.0

P.Majumder, D.J.Patel, C.F.Baca, L.A.Marraffini, J.H.Hickling, L.Ye, S.F.Brady, M.Teplova. The Crispr Associated Adenosine Deaminase CAD1 Converts Atp to Itp to Provide Antiviral Immunity Cell(Cambridge,Mass.) 2024.
ISSN: ISSN 0092-8674
DOI: 10.1016/J.CELL.2024.10.002