Copper in PDB 7og7: Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans

The structure of Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans, PDB code: 7og7 was solved by B.Prasser, L.Schoener, L.Zhang, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.77 / 1.85
Space group	F 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	179.066, 179.066, 179.066, 90, 90, 90
R / Rfree (%)	19.4 / 22.2

The structure of Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Copper atom in the Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans (pdb code 7og7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans, PDB code: 7og7:

Copper binding site 1 out of 1 in the Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Copper Chaperone Nosl From Shewanella Denitrificans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:35.8 occ:1.00 SG A:CYS62 2.3 25.8 1.0 SD A:MET64 2.4 30.2 1.0 SD A:MET145 2.4 31.1 1.0 CG A:MET64 3.3 29.1 1.0 CE A:MET145 3.3 33.4 1.0 CB A:CYS62 3.3 28.7 1.0 CE A:MET64 3.3 34.5 1.0 CG A:MET145 3.5 33.5 1.0 ZN A:ZN202 3.6 34.1 1.0 CB A:MET64 3.6 29.5 1.0 SG A:CYS88 3.9 25.6 1.0 OD2 A:ASP92 4.3 27.4 1.0 O A:ALA144 4.6 34.3 1.0 N A:MET64 4.7 28.6 1.0 CA A:CYS62 4.7 28.2 1.0 CB A:CYS88 4.8 25.6 1.0 O A:CYS62 4.8 30.7 1.0 CA A:MET64 4.8 29.9 1.0 CB A:MET145 4.9 33.4 1.0 C A:CYS62 4.9 32.8 1.0

B.Prasser, L.Schoner, L.Zhang, O.Einsle. The Copper Chaperone Nosl Forms A Heterometal Site For Cu Delivery to Nitrous Oxide Reductase. Angew.Chem.Int.Ed.Engl. 2021.
ISSN: ESSN 1521-3773
PubMed: 34171184
DOI: 10.1002/ANIE.202106348