Zinc in PDB 7sq0: GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1

The structure of GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1 also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1 (pdb code 7sq0). 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 GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1, PDB code: 7sq0:

Zinc binding site 1 out of 1 in the GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of GET3 Bound to Adp and the Transmembrane Domain of the Tail-Anchored Protein BOS1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:125.8 occ:1.00 SG B:CYS290 2.4 79.4 1.0 SG A:CYS290 2.4 79.8 1.0 SG A:CYS287 2.4 78.5 1.0 SG B:CYS287 2.4 78.2 1.0 HB2 A:CYS287 2.9 78.5 1.0 HB2 B:CYS287 2.9 78.2 1.0 CB A:CYS287 3.0 78.5 1.0 CB B:CYS287 3.0 78.2 1.0 HB3 A:CYS287 3.0 78.5 1.0 HB3 B:CYS287 3.0 78.2 1.0 HG B:CYS290 3.0 79.4 1.0 HG A:CYS290 3.1 79.8 1.0 HG A:CYS287 3.1 78.5 1.0 HG B:CYS287 3.1 78.2 1.0 H A:CYS290 3.7 79.8 1.0 H B:CYS290 3.7 79.4 1.0 CB A:CYS290 3.9 79.8 1.0 CB B:CYS290 3.9 79.4 1.0 HB2 A:CYS290 3.9 79.8 1.0 HB2 B:CYS290 3.9 79.4 1.0 HB3 B:MET289 4.2 77.1 1.0 HB3 A:MET289 4.2 77.0 1.0 N A:CYS290 4.4 79.8 1.0 N B:CYS290 4.4 79.4 1.0 CA A:CYS287 4.5 78.5 1.0 CA B:CYS287 4.5 78.2 1.0 HB3 A:CYS290 4.5 79.8 1.0 HB3 B:CYS290 4.5 79.4 1.0 CA A:CYS290 4.8 79.8 1.0 CA B:CYS290 4.8 79.4 1.0 HA A:CYS287 4.8 78.5 1.0 HA B:CYS287 4.8 78.2 1.0

M.Y.Fry, V.Najdrova, A.O.Maggiolo, S.M.Saladi, P.Dolezal, W.M.Clemons Jr.. Structurally Derived Universal Mechanism For the Catalytic Cycle of the Tail-Anchored Targeting Factor GET3. Nat.Struct.Mol.Biol. V. 29 820 2022.
ISSN: ESSN 1545-9985
PubMed: 35851188
DOI: 10.1038/S41594-022-00798-4