Manganese in PDB 7lrc: Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement

All present enzymatic activity of Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement:
3.1.4.17;

The structure of Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Manganese atom in the Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement (pdb code 7lrc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement, PDB code: 7lrc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn2001 b:48.0 occ:1.00 OD1 B:ASP950 1.8 34.0 1.0 OD2 B:ASP837 2.0 30.7 1.0 CG B:ASP950 2.6 34.0 1.0 CG B:ASP837 2.7 30.7 1.0 CD2 B:HIS836 2.8 28.6 1.0 OD2 B:ASP950 2.9 34.0 1.0 OD1 B:ASP837 2.9 30.7 1.0 MG B:MG2002 3.0 29.2 1.0 NE2 B:HIS756 3.1 32.3 1.0 NE2 B:HIS836 3.3 28.6 1.0 CD2 B:HIS756 3.8 32.3 1.0 CB B:ASP950 4.0 34.0 1.0 CG B:HIS836 4.0 28.6 1.0 CB B:ASP837 4.1 30.7 1.0 CE1 B:HIS756 4.2 32.3 1.0 CD2 B:HIS752 4.6 32.5 1.0 CE1 B:HIS836 4.6 28.6 1.0 O B:ASP950 4.7 34.0 1.0 CA B:ASP950 4.8 34.0 1.0 CB B:HIS836 4.8 28.6 1.0 NE2 B:HIS752 4.9 32.5 1.0 ND1 B:HIS836 5.0 28.6 1.0 N B:ASP837 5.0 30.7 1.0 CA B:ASP837 5.0 30.7 1.0

Manganese binding site 2 out of 2 in the Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Cryo-Em of the SLFN12-PDE3A Complex: PDE3A Body Refinement within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn2001 b:48.9 occ:1.00 OD1 C:ASP950 1.8 34.0 1.0 OD2 C:ASP837 2.0 30.8 1.0 CG C:ASP950 2.6 34.0 1.0 CG C:ASP837 2.7 30.8 1.0 CD2 C:HIS836 2.8 28.6 1.0 OD2 C:ASP950 2.9 34.0 1.0 OD1 C:ASP837 2.9 30.8 1.0 MG C:MG2002 3.0 29.1 1.0 NE2 C:HIS756 3.1 32.2 1.0 NE2 C:HIS836 3.3 28.6 1.0 CD2 C:HIS756 3.8 32.2 1.0 CB C:ASP950 4.0 34.0 1.0 CG C:HIS836 4.0 28.6 1.0 CB C:ASP837 4.1 30.8 1.0 CE1 C:HIS756 4.2 32.2 1.0 CD2 C:HIS752 4.6 32.5 1.0 CE1 C:HIS836 4.6 28.6 1.0 O C:ASP950 4.7 34.0 1.0 CA C:ASP950 4.8 34.0 1.0 CB C:HIS836 4.8 28.6 1.0 NE2 C:HIS752 4.9 32.5 1.0 ND1 C:HIS836 5.0 28.6 1.0 N C:ASP837 5.0 30.8 1.0 CA C:ASP837 5.0 30.8 1.0

C.W.Garvie, J.R.Fuller, C.W.Garvie, C.T.Lemke. N/A N/A.