Zinc in PDB 5jb3: Cryo-Em Structure of A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation

The structure of Cryo-Em Structure of A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Cryo-Em Structure of A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation (pdb code 5jb3). 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 Cryo-Em Structure of A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation, PDB code: 5jb3:

Zinc binding site 1 out of 1 in the Cryo-Em Structure of A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation


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 A Full Archaeal Ribosomal Translation Initiation Complex in the P-Remote Conformation within 5.0Å range: probe atom residue distance (Å) B Occ 8:Zn201 b:40.0 occ:1.00 SG 8:CYS127 1.1 40.0 1.0 CB 8:CYS127 2.5 40.0 1.0 CG2 8:THR114 2.7 40.0 1.0 CB 8:CYS106 2.9 40.0 1.0 CA 8:CYS127 3.1 40.0 1.0 O 8:ASP113 3.6 40.0 1.0 CB 8:SER111 3.8 40.0 1.0 SG 8:CYS106 3.9 40.0 1.0 N 8:CYS127 4.0 40.0 1.0 CA 8:CYS106 4.1 40.0 1.0 N 8:CYS106 4.1 40.0 1.0 C 8:ASP113 4.1 40.0 1.0 CB 8:THR114 4.2 40.0 1.0 N 8:ASP113 4.3 40.0 1.0 C 8:CYS127 4.3 40.0 1.0 N 8:LEU112 4.4 40.0 1.0 N 8:SER111 4.4 40.0 1.0 CA 8:SER111 4.5 40.0 1.0 N 8:LEU128 4.5 40.0 1.0 N 8:THR114 4.6 40.0 1.0 CA 8:THR114 4.6 40.0 1.0 C 8:SER111 4.8 40.0 1.0 CA 8:ASP113 4.8 40.0 1.0 O 8:VAL104 4.8 40.0 1.0 C 8:VAL126 4.9 40.0 1.0 OG 8:SER111 4.9 40.0 1.0

P.D.Coureux, C.Lazennec-Schurdevin, A.Monestier, E.Larquet, L.Cladiere, B.P.Klaholz, E.Schmitt, Y.Mechulam. Cryo-Em Study of Start Codon Selection During Archaeal Translation Initiation. Nat Commun V. 7 13366 2016.
ISSN: ESSN 2041-1723
PubMed: 27819266
DOI: 10.1038/NCOMMS13366