Zinc in PDB 7zel: Human SLFN11 Dimer Apoenzyme

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

Magnesium

(Mg)

2 atoms

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

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human SLFN11 Dimer Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:79.0 occ:1.00 SG A:CYS321 2.3 35.7 1.0 ND1 A:HIS285 2.3 37.8 1.0 SG A:CYS287 2.3 53.1 1.0 SG A:CYS322 3.0 36.8 1.0 CE1 A:HIS285 3.2 37.8 1.0 CG A:HIS285 3.4 37.8 1.0 CB A:CYS321 3.6 35.7 1.0 O A:PRO289 3.6 58.5 1.0 CB A:HIS285 3.7 37.8 1.0 CB A:CYS287 3.9 53.1 1.0 CB A:CYS322 4.0 36.8 1.0 CA A:HIS285 4.2 37.8 1.0 NE2 A:HIS285 4.4 37.8 1.0 N A:CYS287 4.4 53.1 1.0 CD2 A:HIS285 4.5 37.8 1.0 C A:CYS321 4.5 35.7 1.0 O A:CYS287 4.5 53.1 1.0 CA A:CYS287 4.5 53.1 1.0 N A:PHE286 4.6 41.0 1.0 C A:CYS287 4.6 53.1 1.0 CA A:CYS321 4.6 35.7 1.0 N A:CYS322 4.6 36.8 1.0 CA A:GLN290 4.7 51.5 1.0 C A:PRO289 4.7 58.5 1.0 O A:CYS321 4.8 35.7 1.0 C A:HIS285 4.9 37.8 1.0 CA A:CYS322 5.0 36.8 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human SLFN11 Dimer Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:73.0 occ:1.00 ND1 B:HIS285 2.1 41.3 1.0 SG B:CYS322 2.3 39.3 1.0 SG B:CYS321 2.3 37.2 1.0 SG B:CYS287 2.3 56.9 1.0 CE1 B:HIS285 2.8 41.3 1.0 CG B:HIS285 3.3 41.3 1.0 CB B:CYS321 3.4 37.2 1.0 CB B:CYS322 3.5 39.3 1.0 CB B:HIS285 3.8 41.3 1.0 CB B:CYS287 3.8 56.9 1.0 NE2 B:HIS285 4.0 41.3 1.0 C B:CYS321 4.0 37.2 1.0 N B:CYS322 4.1 39.3 1.0 O B:PRO289 4.1 62.2 1.0 CA B:HIS285 4.1 41.3 1.0 CD2 B:HIS285 4.3 41.3 1.0 CA B:CYS321 4.3 37.2 1.0 N B:CYS287 4.3 56.9 1.0 N B:PHE286 4.4 44.4 1.0 O B:CYS321 4.4 37.2 1.0 CA B:CYS322 4.4 39.3 1.0 CA B:CYS287 4.5 56.9 1.0 O B:CYS287 4.6 56.9 1.0 C B:HIS285 4.8 41.3 1.0 C B:CYS287 4.8 56.9 1.0 CE2 B:PHE320 4.9 33.3 1.0 N B:CYS321 5.0 37.2 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