Magnesium in PDB 7zel: Human SLFN11 Dimer Apoenzyme

The structure of Human SLFN11 Dimer Apoenzyme also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Human SLFN11 Dimer Apoenzyme (pdb code 7zel). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human SLFN11 Dimer Apoenzyme, PDB code: 7zel:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human SLFN11 Dimer Apoenzyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human SLFN11 Dimer Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:38.8 occ:1.00 OE2 A:GLU214 2.3 31.3 1.0 OE1 A:GLU209 2.7 33.2 1.0 OE2 A:GLU209 2.9 33.2 1.0 CD A:GLU209 3.2 33.2 1.0 CD A:GLU214 3.3 31.3 1.0 OD2 A:ASP252 3.3 56.5 1.0 OE1 A:GLU214 3.5 31.3 1.0 O A:PHE215 4.1 35.9 1.0 NZ A:LYS216 4.3 44.8 1.0 CG A:ASP252 4.5 56.5 1.0 CE A:LYS216 4.6 44.8 1.0 CG A:GLU214 4.6 31.3 1.0 CG A:GLU209 4.7 33.2 1.0 O A:THR138 4.7 23.4 1.0

Magnesium binding site 2 out of 2 in the Human SLFN11 Dimer Apoenzyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human SLFN11 Dimer Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:39.5 occ:1.00 OE2 B:GLU214 2.1 30.4 1.0 OE1 B:GLU209 2.7 33.0 1.0 OE2 B:GLU209 2.8 33.0 1.0 CD B:GLU214 2.9 30.4 1.0 CD B:GLU209 3.1 33.0 1.0 OE1 B:GLU214 3.1 30.4 1.0 O B:PHE215 4.1 35.4 1.0 CG B:GLU214 4.3 30.4 1.0 NZ B:LYS216 4.5 43.8 1.0 OD2 B:ASP252 4.5 54.9 1.0 CE B:LYS216 4.6 43.8 1.0 CG B:GLU209 4.6 33.0 1.0 O B:THR138 4.7 21.8 1.0 CG B:ASP252 4.8 54.9 1.0 OH B:TYR234 4.8 29.8 1.0 N B:PHE215 4.8 35.4 1.0 OD1 B:ASP252 4.9 54.9 1.0

F.J.Metzner, S.J.Wenzl, M.Kugler, S.Krebs, K.P.Hopfner, K.Lammens. Mechanistic Understanding of Human SLFN11. Nat Commun V. 13 5464 2022.
ISSN: ESSN 2041-1723
PubMed: 36115853
DOI: 10.1038/S41467-022-33123-0