Zinc in PDB 5uz4: The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly

The binding sites of Zinc atom in the The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly (pdb code 5uz4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly, PDB code: 5uz4:

Zinc binding site 1 out of 1 in the The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly within 5.0Å range: probe atom residue distance (Å) B Occ Z:Zn401 b:30.5 occ:1.00 ND1 Z:HIS304 2.0 0.0 1.0 SG Z:CYS302 2.4 0.0 1.0 SG Z:CYS310 2.4 0.0 1.0 SG Z:CYS297 2.6 0.0 1.0 CE1 Z:HIS304 3.0 0.0 1.0 CG Z:HIS304 3.0 0.0 1.0 CA Z:HIS304 3.3 0.0 1.0 CB Z:HIS304 3.3 0.0 1.0 O Z:CYS302 3.5 0.0 1.0 N Z:HIS304 3.5 0.0 1.0 CB Z:CYS302 3.7 0.0 1.0 CB Z:CYS297 3.7 0.0 1.0 CB Z:CYS310 3.7 0.0 1.0 N Z:ALA311 3.9 0.0 1.0 NE2 Z:HIS304 4.1 0.0 1.0 CD2 Z:HIS304 4.1 0.0 1.0 CA Z:CYS310 4.1 0.0 1.0 C Z:CYS302 4.1 0.0 1.0 N Z:ILE312 4.3 0.0 1.0 C Z:CYS310 4.5 0.0 1.0 CA Z:CYS302 4.6 0.0 1.0 CG1 Z:ILE312 4.6 30.0 1.0 C Z:LYS303 4.6 0.0 1.0 C Z:HIS304 4.7 0.0 1.0 CB Z:ILE312 4.7 30.0 1.0 CD1 Z:ILE312 4.8 30.0 1.0 CA Z:ALA311 4.8 0.0 1.0 CB Z:ALA311 5.0 0.0 1.0

A.Razi, A.Guarne, J.Ortega. The Cryo-Em Structure of Yjeq Bound to the 30S Subunit Suggests A Fidelity Checkpoint Function For This Protein in Ribosome Assembly. Proc. Natl. Acad. Sci. V. 114 E3396 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28396444
DOI: 10.1073/PNAS.1618016114