Copper in PDB 6wz3: Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3

The structure of Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3, PDB code: 6wz3 was solved by F.A.Tezcan, A.Kakkis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.18 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	78.447, 81.205, 56.431, 90.00, 92.92, 90.00
R / Rfree (%)	18.8 / 23.6

The structure of Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3 also contains other interesting chemical elements:

Iron	(Fe)	3 atoms
Chlorine	(Cl)	7 atoms

The binding sites of Copper atom in the Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3 (pdb code 6wz3). 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 Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3, PDB code: 6wz3:

Copper binding site 1 out of 1 in the Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu-Bound Structure of the Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu206 b:22.1 occ:0.81 NE2 C:HIS73 2.1 22.5 1.0 NE2 A:HIS73 2.1 24.1 1.0 NE2 B:HIS73 2.2 24.6 1.0 NE2 C:HIS77 2.3 37.7 1.0 NE2 A:HIS77 2.3 35.6 1.0 NE2 B:HIS77 2.4 35.8 1.0 CE1 C:HIS73 3.0 28.6 1.0 CE1 C:HIS77 3.1 37.4 1.0 CD2 A:HIS73 3.1 24.8 1.0 CE1 A:HIS73 3.1 31.1 1.0 CE1 A:HIS77 3.1 41.2 1.0 CD2 B:HIS73 3.1 24.7 1.0 CD2 C:HIS73 3.2 23.7 1.0 CE1 B:HIS77 3.2 40.2 1.0 CE1 B:HIS73 3.2 30.6 1.0 CD2 C:HIS77 3.4 35.4 1.0 CD2 B:HIS77 3.5 37.2 1.0 CD2 A:HIS77 3.5 34.6 1.0 ND1 C:HIS73 4.2 29.0 1.0 ND1 A:HIS73 4.2 31.5 1.0 ND1 C:HIS77 4.3 46.6 1.0 CG A:HIS73 4.3 21.7 1.0 CG C:HIS73 4.3 22.8 1.0 ND1 B:HIS73 4.3 30.2 1.0 CG B:HIS73 4.3 22.4 1.0 ND1 A:HIS77 4.3 44.1 1.0 ND1 B:HIS77 4.4 46.3 1.0 CG C:HIS77 4.5 40.1 1.0 CG A:HIS77 4.5 40.6 1.0 CG B:HIS77 4.5 41.8 1.0

F.A.Tezcan, A.Kakkis, D.Gagnon, J.Esselborn, R.D.Britt. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32830423
DOI: 10.1002/ANIE.202009226