Zinc 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:

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

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State), PDB code: 9gmw:
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 (Pre-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 (Pre-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:105.2 occ:1.00 ND1 A:HIS285 2.1 52.4 1.0 SG A:CYS322 2.3 68.5 1.0 SG A:CYS321 2.3 62.2 1.0 SG A:CYS287 2.3 81.3 1.0 CE1 A:HIS285 2.8 52.2 1.0 CG A:HIS285 3.2 54.7 1.0 CB A:CYS321 3.4 55.0 1.0 CB A:CYS322 3.5 55.2 1.0 CB A:HIS285 3.7 57.8 1.0 CB A:CYS287 3.9 74.8 1.0 CA A:HIS285 4.0 56.7 1.0 NE2 A:HIS285 4.0 53.5 1.0 C A:CYS321 4.0 49.2 1.0 N A:CYS322 4.1 57.4 1.0 N A:PHE286 4.2 48.7 1.0 CD2 A:HIS285 4.2 53.0 1.0 CA A:CYS321 4.3 51.3 1.0 CA A:CYS322 4.4 54.4 1.0 O A:CYS321 4.4 48.3 1.0 N A:CYS287 4.4 75.1 1.0 O A:PRO289 4.6 76.6 1.0 CA A:CYS287 4.7 75.9 1.0 C A:HIS285 4.7 55.2 1.0 O A:CYS287 4.9 74.0 1.0 C A:CYS287 5.0 77.1 1.0 N A:CYS321 5.0 57.0 1.0

Zinc binding site 2 out of 2 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-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 (Pre-Cleavage State) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:101.5 occ:1.00 ND1 B:HIS285 2.1 59.6 1.0 SG B:CYS322 2.3 77.6 1.0 SG B:CYS321 2.3 69.1 1.0 SG B:CYS287 2.3 83.1 1.0 CE1 B:HIS285 2.8 58.6 1.0 CG B:HIS285 3.3 59.5 1.0 CB B:CYS321 3.4 60.1 1.0 CB B:CYS322 3.6 58.5 1.0 CB B:HIS285 3.8 58.6 1.0 CB B:CYS287 3.9 74.7 1.0 C B:CYS321 4.0 54.0 1.0 NE2 B:HIS285 4.0 58.1 1.0 N B:CYS322 4.1 57.5 1.0 CA B:HIS285 4.2 56.3 1.0 CD2 B:HIS285 4.3 55.1 1.0 CA B:CYS321 4.3 55.6 1.0 O B:CYS321 4.3 50.0 1.0 N B:PHE286 4.4 62.5 1.0 O B:PRO289 4.5 86.1 1.0 N B:CYS287 4.5 81.0 1.0 CA B:CYS322 4.5 57.5 1.0 CA B:CYS287 4.7 76.9 1.0 C B:HIS285 4.9 58.5 1.0 N B:CYS321 5.0 57.7 1.0 C B:CYS287 5.0 80.8 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