Manganese in PDB 6wz1: Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3

The structure of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz1 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)	34.79 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.759, 77.392, 47.940, 90.00, 110.70, 90.00
R / Rfree (%)	17.6 / 22.9

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

Iron	(Fe)	3 atoms
Calcium	(Ca)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Manganese atom in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 (pdb code 6wz1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz1:

Manganese binding site 1 out of 1 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:8.4 occ:0.72 NE2 B:HIS73 2.2 33.0 1.0 NE2 C:HIS73 2.2 25.7 1.0 NE2 A:HIS73 2.2 26.1 1.0 NE2 A:HIS77 2.3 27.4 0.5 NE2 C:HIS77 2.3 31.5 1.0 NE2 B:HIS77 2.5 40.7 0.5 CE1 B:HIS73 2.8 30.0 1.0 CE1 C:HIS73 2.9 32.5 1.0 CE1 A:HIS77 2.9 28.6 0.5 CE1 C:HIS77 2.9 40.0 1.0 CE1 A:HIS73 3.0 23.6 1.0 CE1 B:HIS77 3.2 35.9 0.5 CD2 A:HIS73 3.4 18.9 1.0 CD2 B:HIS73 3.4 25.0 1.0 CD2 C:HIS73 3.4 21.3 1.0 CD2 C:HIS77 3.5 30.1 1.0 CD2 A:HIS77 3.6 26.9 0.5 CD2 B:HIS77 3.6 34.6 0.5 ND1 B:HIS73 4.1 28.9 1.0 ND1 C:HIS73 4.1 23.3 1.0 ND1 A:HIS77 4.1 29.9 0.5 ND1 C:HIS77 4.2 42.9 1.0 ND1 A:HIS73 4.2 28.5 1.0 CG B:HIS73 4.3 28.0 1.0 CG C:HIS73 4.4 22.1 1.0 CG A:HIS73 4.4 23.8 1.0 ND1 B:HIS77 4.4 34.5 0.5 CG C:HIS77 4.5 33.4 1.0 CG A:HIS77 4.5 26.1 0.5 ND1 A:HIS77 4.5 27.4 0.5 CG B:HIS77 4.6 30.9 0.5 CE1 A:HIS77 4.7 30.0 0.5 O B:HOH306 4.9 35.2 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