Zinc in PDB 9ere: SLFN11 Dimer Bound to Trna-Leu-Taa

The structure of SLFN11 Dimer Bound to Trna-Leu-Taa also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Manganese	(Mn)	3 atoms

The binding sites of Zinc atom in the SLFN11 Dimer Bound to Trna-Leu-Taa (pdb code 9ere). 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 Dimer Bound to Trna-Leu-Taa, PDB code: 9ere:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the SLFN11 Dimer Bound to Trna-Leu-Taa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of SLFN11 Dimer Bound to Trna-Leu-Taa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:87.5 occ:1.00 ND1 A:HIS285 2.1 42.0 1.0 SG A:CYS322 2.3 53.2 1.0 SG A:CYS321 2.3 50.2 1.0 SG A:CYS287 2.3 55.3 1.0 CE1 A:HIS285 2.9 40.9 1.0 CG A:HIS285 3.2 44.0 1.0 CB A:CYS321 3.4 38.3 1.0 CB A:CYS322 3.5 41.1 1.0 CB A:HIS285 3.7 44.0 1.0 CB A:CYS287 3.8 52.3 1.0 CA A:HIS285 4.0 39.8 1.0 NE2 A:HIS285 4.1 39.2 1.0 N A:CYS322 4.1 39.1 1.0 C A:CYS321 4.1 35.8 1.0 CD2 A:HIS285 4.3 37.4 1.0 CA A:CYS321 4.3 36.3 1.0 N A:PHE286 4.3 37.9 1.0 O A:PRO289 4.4 59.1 1.0 CA A:CYS322 4.4 37.8 1.0 N A:CYS287 4.5 52.0 1.0 O A:CYS321 4.5 38.9 1.0 CA A:CYS287 4.6 54.2 1.0 C A:HIS285 4.7 39.7 1.0 N A:CYS321 4.9 42.3 1.0 C A:CYS287 5.0 59.5 1.0

Zinc binding site 2 out of 2 in the SLFN11 Dimer Bound to Trna-Leu-Taa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of SLFN11 Dimer Bound to Trna-Leu-Taa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:84.2 occ:1.00 ND1 B:HIS285 2.1 43.8 1.0 SG B:CYS321 2.3 47.9 1.0 SG B:CYS322 2.3 48.2 1.0 SG B:CYS287 2.3 62.2 1.0 CE1 B:HIS285 3.0 43.4 1.0 CG B:HIS285 3.2 44.0 1.0 CB B:CYS321 3.3 41.6 1.0 CB B:CYS322 3.6 41.9 1.0 CB B:HIS285 3.6 43.0 1.0 CB B:CYS287 3.8 57.5 1.0 CA B:HIS285 3.9 40.4 1.0 N B:CYS322 4.1 42.5 1.0 C B:CYS321 4.1 38.8 1.0 NE2 B:HIS285 4.1 39.4 1.0 N B:CYS287 4.2 58.8 1.0 N B:PHE286 4.2 41.2 1.0 CD2 B:HIS285 4.3 39.9 1.0 CA B:CYS321 4.3 39.0 1.0 O B:PRO289 4.3 63.0 1.0 CA B:CYS322 4.4 40.5 1.0 CA B:CYS287 4.5 56.5 1.0 O B:CYS321 4.6 40.1 1.0 C B:HIS285 4.6 40.7 1.0 O B:CYS287 4.8 60.5 1.0 C B:CYS287 4.8 60.7 1.0 N B:CYS321 4.9 40.9 1.0 CE2 B:PHE320 5.0 36.2 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