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

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

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

The binding sites of Manganese atom in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) (pdb code 9gmw). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State), PDB code: 9gmw:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-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 (Pre-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1002 b:68.1 occ:1.00 OD2 A:ASP252 2.0 57.5 1.0 OE2 A:GLU214 2.1 49.6 1.0 OP1 T:U65 2.4 64.0 1.0 OE2 A:GLU209 2.5 53.1 1.0 O A:PHE215 2.6 43.6 1.0 CG A:ASP252 3.1 55.2 1.0 CD A:GLU214 3.2 43.5 1.0 CD A:GLU209 3.3 51.6 1.0 OE1 A:GLU209 3.4 56.4 1.0 C A:PHE215 3.8 38.0 1.0 P T:U65 3.8 62.9 1.0 OE1 A:GLU214 3.9 41.7 1.0 CD A:LYS216 4.0 43.7 1.0 OD1 A:ASP252 4.0 54.8 1.0 CB A:ASP252 4.0 52.5 1.0 N A:PHE215 4.2 37.0 1.0 CG A:GLU214 4.3 39.3 1.0 C5' T:U65 4.3 52.4 1.0 O5' T:U65 4.3 55.5 1.0 OP2 T:C66 4.3 56.9 1.0 CA A:PHE215 4.5 33.5 1.0 NZ A:LYS216 4.7 48.2 1.0 OP2 T:U65 4.7 49.9 1.0 O3' T:U64 4.8 49.8 1.0 CG A:GLU209 4.8 42.9 1.0 CB A:PHE215 4.8 45.3 1.0 N A:LYS216 4.9 38.6 1.0 CG A:LYS216 5.0 43.6 1.0 CA A:ASP252 5.0 50.9 1.0 CE A:LYS216 5.0 43.3 1.0 OP1 T:C66 5.0 56.6 1.0

Manganese binding site 2 out of 3 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-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 (Pre-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1002 b:56.1 occ:1.00 OE2 B:GLU214 2.1 54.2 1.0 O B:PHE215 2.2 59.4 1.0 OD2 B:ASP252 2.3 67.3 1.0 OE2 B:GLU209 2.3 52.1 1.0 OP1 T:C77 2.4 76.5 1.0 MN B:MN1003 2.8 74.1 1.0 CD B:GLU214 3.3 49.3 1.0 CD B:GLU209 3.3 51.1 1.0 C B:PHE215 3.3 53.5 1.0 CG B:ASP252 3.5 73.0 1.0 OE1 B:GLU209 3.6 55.3 1.0 P T:C77 3.8 89.9 1.0 N B:PHE215 3.8 48.0 1.0 CD B:LYS216 3.9 58.4 1.0 OD1 B:ASP252 4.0 70.9 1.0 CE B:LYS216 4.0 57.8 1.0 CA B:PHE215 4.0 43.1 1.0 CG B:GLU214 4.1 47.8 1.0 OE1 B:GLU214 4.1 43.9 1.0 O5' T:C77 4.2 83.7 1.0 C5' T:C77 4.2 78.1 1.0 NZ B:LYS216 4.3 59.3 1.0 CB B:PHE215 4.4 53.3 1.0 N B:LYS216 4.4 60.3 1.0 CG B:LYS216 4.6 57.8 1.0 CB B:ASP252 4.6 73.3 1.0 CA B:LYS216 4.7 56.1 1.0 CG B:GLU209 4.7 44.8 1.0 O3' T:U76 4.7 70.1 1.0 OP2 T:C77 4.8 80.4 1.0 C B:GLU214 4.9 50.2 1.0

Manganese binding site 3 out of 3 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1003 b:74.1 occ:1.00 OE1 B:GLU209 2.0 55.3 1.0 OP1 T:C77 2.6 76.5 1.0 CD B:GLU209 2.8 51.1 1.0 OE2 B:GLU214 2.8 54.2 1.0 MN B:MN1002 2.8 56.1 1.0 OE2 B:GLU209 2.9 52.1 1.0 OE1 B:GLU214 3.5 43.9 1.0 CD B:GLU214 3.5 49.3 1.0 P T:C77 3.7 89.9 1.0 O3' T:U76 3.7 70.1 1.0 OD2 B:ASP252 3.9 67.3 1.0 O B:THR138 4.1 53.2 1.0 OD1 B:ASP252 4.2 70.9 1.0 CG B:GLU209 4.2 44.8 1.0 CG B:ASP252 4.5 73.0 1.0 CB B:GLU209 4.7 43.1 1.0 OP2 T:C77 4.7 80.4 1.0 O5' T:C77 4.8 83.7 1.0 C5' T:C77 4.9 78.1 1.0 O B:PHE215 4.9 59.4 1.0 CG B:GLU214 5.0 47.8 1.0 C3' T:U76 5.0 62.4 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