Zinc in PDB 8oh9: Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1)

The structure of Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) also contains other interesting chemical elements:

Iron

(Fe)

168 atoms

The binding sites of Zinc atom in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) (pdb code 8oh9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1), PDB code: 8oh9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1)


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 the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:99.3 occ:1.00 NE2 B:HIS512 2.3 64.5 1.0 SG B:CYS523 2.3 70.4 1.0 SG B:CYS518 2.3 70.2 1.0 CB B:CYS518 2.5 70.2 1.0 CB B:CYS523 3.0 70.4 1.0 CD2 B:HIS512 3.1 64.5 1.0 CE1 B:HIS512 3.2 64.5 1.0 CA B:CYS518 3.6 70.2 1.0 CD1 B:LEU526 3.6 69.7 1.0 SG B:CYS425 3.7 66.0 1.0 N B:CYS523 3.9 70.4 1.0 CA B:CYS523 4.0 70.4 1.0 CB B:CYS425 4.1 66.0 1.0 OG B:SER522 4.1 67.2 1.0 CG B:HIS512 4.2 64.5 1.0 ND1 B:HIS512 4.2 64.5 1.0 N B:CYS518 4.5 70.2 1.0 C B:CYS518 4.7 70.2 1.0 CG B:LEU526 4.7 69.7 1.0 CB B:LEU526 4.8 69.7 1.0 C B:SER522 5.0 67.2 1.0

Zinc binding site 2 out of 4 in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1)


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 the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn601 b:98.0 occ:1.00 NE2 E:HIS512 2.3 64.7 1.0 SG E:CYS523 2.3 69.7 1.0 SG E:CYS518 2.3 70.6 1.0 CB E:CYS518 2.5 70.6 1.0 CB E:CYS523 3.0 69.7 1.0 CD2 E:HIS512 3.1 64.7 1.0 CE1 E:HIS512 3.2 64.7 1.0 SG E:CYS425 3.6 65.8 1.0 CA E:CYS518 3.6 70.6 1.0 CD1 E:LEU526 3.6 69.5 1.0 N E:CYS523 3.9 69.7 1.0 CA E:CYS523 4.0 69.7 1.0 CB E:CYS425 4.1 65.8 1.0 OG E:SER522 4.1 67.4 1.0 CG E:HIS512 4.2 64.7 1.0 ND1 E:HIS512 4.2 64.7 1.0 N E:CYS518 4.6 70.6 1.0 C E:CYS518 4.7 70.6 1.0 CG E:LEU526 4.7 69.5 1.0 CB E:LEU526 4.8 69.5 1.0 C E:SER522 5.0 67.4 1.0

Zinc binding site 3 out of 4 in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1)


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 the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn601 b:93.4 occ:1.00 NE2 H:HIS512 2.3 63.9 1.0 SG H:CYS523 2.3 68.5 1.0 SG H:CYS518 2.3 69.1 1.0 CB H:CYS518 2.6 69.1 1.0 CB H:CYS523 3.1 68.5 1.0 CD2 H:HIS512 3.2 63.9 1.0 CE1 H:HIS512 3.2 63.9 1.0 SG H:CYS425 3.5 66.4 1.0 CA H:CYS518 3.7 69.1 1.0 CD1 H:LEU526 3.7 68.5 1.0 N H:CYS523 3.9 68.5 1.0 CB H:CYS425 3.9 66.4 1.0 OG H:SER522 4.1 66.8 1.0 CA H:CYS523 4.1 68.5 1.0 ND1 H:HIS512 4.3 63.9 1.0 CG H:HIS512 4.3 63.9 1.0 N H:CYS518 4.6 69.1 1.0 C H:CYS518 4.7 69.1 1.0 CG H:LEU526 4.8 68.5 1.0 CB H:LEU526 4.8 68.5 1.0 C H:SER522 4.9 66.8 1.0

Zinc binding site 4 out of 4 in the Cryo-Em Structure of the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1)


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 the Electron Bifurcating Transhydrogenase Stnabc Complex From Sporomusa Ovata (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ K:Zn601 b:101.9 occ:1.00 NE2 K:HIS512 2.3 64.7 1.0 SG K:CYS523 2.3 69.5 1.0 SG K:CYS518 2.3 70.9 1.0 CB K:CYS518 2.6 70.9 1.0 CB K:CYS523 3.0 69.5 1.0 CD2 K:HIS512 3.1 64.7 1.0 CE1 K:HIS512 3.2 64.7 1.0 CD1 K:LEU526 3.6 69.4 1.0 CA K:CYS518 3.7 70.9 1.0 SG K:CYS425 3.7 65.1 1.0 N K:CYS523 3.8 69.5 1.0 OG K:SER522 4.0 66.3 1.0 CA K:CYS523 4.0 69.5 1.0 CB K:CYS425 4.0 65.1 1.0 CG K:HIS512 4.2 64.7 1.0 ND1 K:HIS512 4.2 64.7 1.0 N K:CYS518 4.6 70.9 1.0 C K:CYS518 4.7 70.9 1.0 CG K:LEU526 4.8 69.4 1.0 CB K:LEU526 4.8 69.4 1.0 C K:SER522 4.9 66.3 1.0 N K:SER522 5.0 66.3 1.0

A.Kumar, F.Kremp, J.Roth, S.A.Freibert, V.Mueller, J.M.Schuller. Molecular Architecture and Electron Transfer Pathway of the Stn Family Transhydrogenase Nat Commun 2023.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-023-41212-X