Zinc in PDB 9erf: SLFN11 Dimer Bound to Trna-Met-Cat

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

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

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

Zinc binding site 1 out of 2 in the SLFN11 Dimer Bound to Trna-Met-Cat


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-Met-Cat within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:74.6 occ:1.00 ND1 A:HIS285 2.1 30.8 1.0 SG A:CYS322 2.3 40.6 1.0 SG A:CYS321 2.3 41.6 1.0 SG A:CYS287 2.3 50.4 1.0 CE1 A:HIS285 2.9 30.8 1.0 CG A:HIS285 3.2 30.2 1.0 CB A:CYS321 3.4 32.5 1.0 CB A:CYS322 3.6 34.3 1.0 CB A:HIS285 3.7 33.5 1.0 CB A:CYS287 3.8 44.4 1.0 CA A:HIS285 4.0 30.8 1.0 NE2 A:HIS285 4.1 32.4 1.0 N A:CYS322 4.1 27.8 1.0 C A:CYS321 4.1 23.9 1.0 O A:PRO289 4.2 52.8 1.0 CD2 A:HIS285 4.3 28.4 1.0 N A:CYS287 4.3 42.9 1.0 CA A:CYS321 4.3 25.6 1.0 N A:PHE286 4.3 30.7 1.0 CA A:CYS322 4.4 27.5 1.0 CA A:CYS287 4.5 44.0 1.0 O A:CYS321 4.6 30.9 1.0 C A:HIS285 4.7 25.6 1.0 C A:CYS287 4.8 50.9 1.0 O A:CYS287 4.9 51.9 1.0 N A:CYS321 5.0 26.7 1.0 CZ A:PHE320 5.0 27.2 1.0

Zinc binding site 2 out of 2 in the SLFN11 Dimer Bound to Trna-Met-Cat


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-Met-Cat within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:79.9 occ:1.00 ND1 B:HIS285 2.1 32.4 1.0 SG B:CYS322 2.3 43.0 1.0 SG B:CYS321 2.3 41.4 1.0 SG B:CYS287 2.3 56.2 1.0 CE1 B:HIS285 2.9 33.4 1.0 CG B:HIS285 3.2 24.4 1.0 CB B:CYS321 3.3 30.5 1.0 CB B:CYS322 3.5 33.1 1.0 CB B:HIS285 3.7 33.0 1.0 CB B:CYS287 3.8 48.3 1.0 CA B:HIS285 4.0 26.3 1.0 N B:CYS322 4.1 31.4 1.0 NE2 B:HIS285 4.1 30.2 1.0 C B:CYS321 4.1 28.2 1.0 N B:CYS287 4.3 49.7 1.0 CA B:CYS321 4.3 29.3 1.0 CD2 B:HIS285 4.3 22.9 1.0 O B:PRO289 4.3 52.9 1.0 CA B:CYS322 4.4 27.5 1.0 N B:PHE286 4.4 31.4 1.0 CA B:CYS287 4.5 46.6 1.0 O B:CYS321 4.6 27.4 1.0 C B:HIS285 4.7 26.8 1.0 N B:CYS321 4.9 34.9 1.0 C B:CYS287 5.0 52.6 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