Cobalt in PDB 6x7e: Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site

The structure of Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site, PDB code: 6x7e 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)	39.70 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.090, 78.003, 50.189, 90.00, 106.48, 90.00
R / Rfree (%)	16.2 / 21.3

The structure of Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site also contains other interesting chemical elements:

Magnesium	(Mg)	6 atoms
Iron	(Fe)	3 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Cobalt atom in the Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site (pdb code 6x7e). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site, PDB code: 6x7e:

Cobalt binding site 1 out of 1 in the Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, with Delta Isomerism at the Hexahistidine Coordination Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Co202 b:16.5 occ:1.00 NE2 A:HIS73 2.2 16.1 1.0 NE2 C:HIS73 2.2 18.7 1.0 NE2 B:HIS73 2.2 20.1 1.0 NE2 A:HIS77 2.3 21.1 1.0 NE2 B:HIS77 2.3 19.5 1.0 NE2 C:HIS77 2.3 24.4 1.0 CD2 B:HIS77 3.1 20.8 1.0 CD2 A:HIS77 3.1 19.3 1.0 CD2 B:HIS73 3.1 15.7 1.0 CD2 A:HIS73 3.1 11.8 1.0 CD2 C:HIS73 3.1 19.6 1.0 CE1 A:HIS73 3.1 21.0 1.0 CE1 C:HIS73 3.2 17.2 1.0 CE1 B:HIS73 3.2 20.8 1.0 CE1 C:HIS77 3.2 33.0 1.0 CD2 C:HIS77 3.3 23.7 1.0 CE1 A:HIS77 3.3 19.7 1.0 CE1 B:HIS77 3.4 19.9 1.0 ND1 A:HIS73 4.2 21.6 1.0 CG B:HIS73 4.2 17.4 1.0 CG B:HIS77 4.3 23.2 1.0 CG A:HIS73 4.3 16.1 1.0 CG A:HIS77 4.3 21.8 1.0 ND1 B:HIS73 4.3 15.0 1.0 ND1 C:HIS73 4.3 19.2 1.0 CG C:HIS73 4.3 20.1 1.0 ND1 C:HIS77 4.3 30.1 1.0 ND1 A:HIS77 4.3 19.4 1.0 CG C:HIS77 4.4 39.0 1.0 ND1 B:HIS77 4.4 18.3 1.0 O B:HOH398 4.7 23.6 1.0 O A:HOH397 4.9 17.4 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