Zinc 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
Manganese	(Mn)	2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Post-Cleavage State), PDB code: 9gmx:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn1001 b:95.7 occ:1.00 ND1 A:HIS285 2.1 50.7 1.0 SG A:CYS322 2.3 63.5 1.0 SG A:CYS321 2.3 51.8 1.0 SG A:CYS287 2.3 66.0 1.0 CE1 A:HIS285 2.8 50.5 1.0 CG A:HIS285 3.2 52.3 1.0 CB A:CYS321 3.3 51.0 1.0 CB A:CYS322 3.5 51.6 1.0 CB A:HIS285 3.7 53.0 1.0 CB A:CYS287 3.8 62.1 1.0 NE2 A:HIS285 4.0 55.2 1.0 N A:CYS322 4.0 47.9 1.0 CA A:HIS285 4.1 51.1 1.0 C A:CYS321 4.1 43.9 1.0 O A:PRO289 4.2 67.4 1.0 CD2 A:HIS285 4.2 50.7 1.0 CA A:CYS321 4.3 43.9 1.0 N A:PHE286 4.3 41.6 1.0 N A:CYS287 4.4 62.1 1.0 CA A:CYS322 4.4 45.6 1.0 O A:CYS321 4.5 48.8 1.0 CA A:CYS287 4.6 64.8 1.0 O A:CYS287 4.7 70.7 1.0 C A:HIS285 4.7 49.3 1.0 C A:CYS287 4.9 68.6 1.0 N A:CYS321 4.9 44.1 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn1001 b:97.2 occ:1.00 ND1 B:HIS285 2.1 48.5 1.0 SG B:CYS321 2.3 56.3 1.0 SG B:CYS322 2.3 60.5 1.0 SG B:CYS287 2.3 73.9 1.0 CE1 B:HIS285 2.9 48.9 1.0 CG B:HIS285 3.1 54.6 1.0 CB B:CYS322 3.4 52.4 1.0 CB B:CYS321 3.4 49.5 1.0 CB B:HIS285 3.6 54.7 1.0 CB B:CYS287 3.8 68.0 1.0 CA B:HIS285 3.8 46.6 1.0 N B:CYS322 4.0 45.0 1.0 N B:PHE286 4.0 52.9 1.0 NE2 B:HIS285 4.1 50.8 1.0 C B:CYS321 4.1 47.7 1.0 CD2 B:HIS285 4.2 50.5 1.0 CA B:CYS322 4.3 46.3 1.0 CA B:CYS321 4.4 49.9 1.0 N B:CYS287 4.4 69.8 1.0 C B:HIS285 4.5 44.9 1.0 O B:CYS321 4.6 52.0 1.0 CA B:CYS287 4.6 67.9 1.0 O B:VAL284 4.7 55.7 1.0 O B:PRO289 4.7 75.5 1.0 C B:PHE286 5.0 53.6 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