Zinc in PDB 7wi4: Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains

The structure of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains also contains other interesting chemical elements:

Magnesium

(Mg)

6 atoms

The binding sites of Zinc atom in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains (pdb code 7wi4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains, PDB code: 7wi4:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:53.7 occ:1.00 OD2 A:ASP492 2.0 47.1 1.0 NE2 A:HIS418 2.3 43.4 1.0 NE2 A:HIS414 2.3 45.6 1.0 CG A:ASP492 2.9 47.1 1.0 CE1 A:HIS418 3.1 43.4 1.0 CE1 A:HIS414 3.2 45.6 1.0 OD1 A:ASP492 3.2 47.1 1.0 CD2 A:HIS414 3.3 45.6 1.0 CD2 A:HIS418 3.4 43.4 1.0 CB A:ASP492 4.2 47.1 1.0 ND1 A:HIS414 4.3 45.6 1.0 ND1 A:HIS418 4.3 43.4 1.0 CG A:HIS414 4.4 45.6 1.0 CG A:HIS418 4.4 43.4 1.0 O A:LEU469 5.0 61.4 1.0 CA A:GLY472 5.0 43.4 1.0

Zinc binding site 2 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn702 b:52.5 occ:1.00 OD2 D:ASP492 1.9 47.5 1.0 CE1 D:HIS414 2.2 45.4 1.0 NE2 D:HIS418 2.3 42.5 1.0 NE2 D:HIS414 2.3 45.4 1.0 CE1 D:HIS418 3.0 42.5 1.0 CG D:ASP492 3.1 47.5 1.0 CD2 D:HIS418 3.2 42.5 1.0 ND1 D:HIS414 3.4 45.4 1.0 CD2 D:HIS414 3.5 45.4 1.0 OD1 D:ASP492 3.8 47.5 1.0 CG D:HIS414 4.0 45.4 1.0 ND1 D:HIS418 4.1 42.5 1.0 CG D:HIS418 4.2 42.5 1.0 CB D:ASP492 4.3 47.5 1.0 O D:HIS414 4.4 45.4 1.0 OE1 D:GLN415 4.5 45.7 1.0 NE2 D:GLN415 4.9 45.7 1.0 CA D:GLY472 5.0 39.1 1.0

Zinc binding site 3 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn702 b:50.0 occ:1.00 OD1 E:ASP492 1.9 45.8 1.0 NE2 E:HIS414 2.3 42.5 1.0 NE2 E:HIS418 2.3 37.2 1.0 CG E:ASP492 3.0 45.8 1.0 CD2 E:HIS414 3.1 42.5 1.0 CD2 E:HIS418 3.2 37.2 1.0 CE1 E:HIS418 3.2 37.2 1.0 CE1 E:HIS414 3.3 42.5 1.0 OD2 E:ASP492 3.4 45.8 1.0 CB E:ASP492 4.3 45.8 1.0 ND1 E:HIS418 4.3 37.2 1.0 CG E:HIS418 4.3 37.2 1.0 CG E:HIS414 4.3 42.5 1.0 ND1 E:HIS414 4.3 42.5 1.0 NE2 E:GLN415 4.6 39.5 1.0 O E:LEU469 4.7 35.8 1.0 CA E:GLY472 5.0 44.5 1.0 N E:GLY472 5.0 44.5 1.0

Zinc binding site 4 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn702 b:56.6 occ:1.00 OD2 F:ASP492 1.8 47.6 1.0 NE2 F:HIS418 2.3 44.4 1.0 NE2 F:HIS414 2.3 42.9 1.0 CG F:ASP492 2.8 47.6 1.0 CE1 F:HIS414 3.2 42.9 1.0 CE1 F:HIS418 3.2 44.4 1.0 CD2 F:HIS414 3.2 42.9 1.0 OD1 F:ASP492 3.2 47.6 1.0 CD2 F:HIS418 3.3 44.4 1.0 CB F:ASP492 4.2 47.6 1.0 ND1 F:HIS414 4.2 42.9 1.0 CG F:HIS414 4.3 42.9 1.0 ND1 F:HIS418 4.3 44.4 1.0 CG F:HIS418 4.4 44.4 1.0 CA F:GLY472 4.9 41.8 1.0

Zinc binding site 5 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn702 b:48.7 occ:1.00 OD2 B:ASP492 2.1 47.2 1.0 NE2 B:HIS418 2.3 33.0 1.0 NE2 B:HIS414 2.3 47.5 1.0 CD2 B:HIS414 3.0 47.5 1.0 CG B:ASP492 3.0 47.2 1.0 CD2 B:HIS418 3.0 33.0 1.0 OD1 B:ASP492 3.2 47.2 1.0 CE1 B:HIS418 3.3 33.0 1.0 CE1 B:HIS414 3.3 47.5 1.0 CG B:HIS414 4.1 47.5 1.0 CG B:HIS418 4.2 33.0 1.0 ND1 B:HIS418 4.2 33.0 1.0 ND1 B:HIS414 4.3 47.5 1.0 CB B:ASP492 4.3 47.2 1.0 CA B:GLY472 4.7 45.0 1.0 OE1 B:GLN415 4.7 43.8 1.0 N B:GLY472 4.9 45.0 1.0 O B:LEU469 4.9 61.4 1.0

Zinc binding site 6 out of 6 in the Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo-Em Structure of E.Coli Ftsh Protease Cytosolic Domains within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn702 b:51.2 occ:1.00 CE1 C:HIS418 1.8 43.7 1.0 OD1 C:ASP492 2.0 47.6 1.0 NE2 C:HIS414 2.3 43.8 1.0 NE2 C:HIS418 2.3 43.7 1.0 ND1 C:HIS418 2.9 43.7 1.0 CG C:ASP492 3.0 47.6 1.0 CD2 C:HIS414 3.2 43.8 1.0 OD2 C:ASP492 3.3 47.6 1.0 CE1 C:HIS414 3.3 43.8 1.0 CD2 C:HIS418 3.5 43.7 1.0 CG C:HIS418 3.8 43.7 1.0 CB C:ASP492 4.3 47.6 1.0 CG C:HIS414 4.4 43.8 1.0 ND1 C:HIS414 4.4 43.8 1.0 O C:LEU469 4.4 35.2 1.0 NE2 C:GLN415 4.9 40.0 1.0

Z.Qiao, T.Yokoyama, X.F.Yan, I.T.Beh, J.Shi, S.Basak, Y.Akiyama, Y.G.Gao. Cryo-Em Structure of the Entire Ftsh-Hflkc Aaa Protease Complex. Cell Rep V. 39 10890 2022.
ISSN: ESSN 2211-1247
PubMed: 35649372
DOI: 10.1016/J.CELREP.2022.110890