Manganese in PDB 9gmx: SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State)

The structure of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State) also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Zinc	(Zn)	2 atoms

The binding sites of Manganese atom in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State) (pdb code 9gmx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State), PDB code: 9gmx:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1002 b:59.0 occ:1.00 OE2 A:GLU214 2.0 36.4 1.0 OD1 A:ASP252 2.1 49.1 1.0 OP1 T:U65 2.5 49.6 1.0 OE2 A:GLU209 2.5 45.2 1.0 O A:PHE215 2.9 32.8 1.0 CG A:ASP252 3.1 50.9 1.0 CD A:GLU214 3.2 34.9 1.0 CD A:GLU209 3.3 37.4 1.0 OE1 A:GLU209 3.4 45.2 1.0 OD2 A:ASP252 3.5 53.5 1.0 OE1 A:GLU214 3.7 41.3 1.0 P T:U65 3.9 51.1 1.0 C A:PHE215 4.0 37.0 1.0 OP2 T:C66 4.1 46.0 1.0 CD A:LYS216 4.3 40.2 1.0 N A:PHE215 4.3 35.6 1.0 CG A:GLU214 4.3 29.4 1.0 CB A:ASP252 4.3 46.1 1.0 C5' T:U65 4.4 36.8 1.0 O5' T:U65 4.5 46.7 1.0 CA A:PHE215 4.7 33.9 1.0 O3' T:U64 4.7 37.6 1.0 CG A:GLU209 4.8 31.8 1.0 NZ A:LYS216 4.9 40.8 1.0 OP2 T:U65 5.0 38.5 1.0

Manganese binding site 2 out of 2 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1002 b:75.3 occ:1.00 OE2 B:GLU214 2.0 54.0 1.0 OD2 B:ASP252 2.1 65.1 1.0 OE2 B:GLU209 2.1 49.0 1.0 O B:PHE215 2.3 57.2 1.0 CD B:GLU214 3.1 47.7 1.0 CD B:GLU209 3.1 51.4 1.0 CG B:ASP252 3.3 67.7 1.0 OE1 B:GLU209 3.4 50.8 1.0 C B:PHE215 3.4 52.3 1.0 N B:PHE215 3.8 45.7 1.0 OE1 B:GLU214 3.9 50.4 1.0 CG B:GLU214 4.0 39.2 1.0 OD1 B:ASP252 4.0 69.0 1.0 CA B:PHE215 4.1 45.5 1.0 CE B:LYS216 4.2 54.5 1.0 CD B:LYS216 4.3 56.0 1.0 CB B:ASP252 4.3 66.0 1.0 OP1 U:C77 4.4 76.9 1.0 CG B:GLU209 4.5 46.9 1.0 N B:LYS216 4.5 52.1 1.0 CB B:PHE215 4.5 49.8 1.0 C B:GLU214 4.6 45.2 1.0 NZ B:LYS216 4.7 53.3 1.0 CG B:LYS216 4.7 51.1 1.0 CA B:LYS216 4.8 52.0 1.0 CA B:GLU214 4.9 36.7 1.0

M.Kugler, F.J.Metzner, K.P.Hopfner, K.Lammens. Phosphorylation-Mediated Conformational Change Regulates Human SLFN11 Nat Commun 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-54833-7