Manganese in PDB 6wz7: Mn-Bound Structure of A TRICYT3 Variant

The structure of Mn-Bound Structure of A TRICYT3 Variant, PDB code: 6wz7 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)	35.40 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.978, 81.847, 53.385, 90.00, 90.04, 90.00
R / Rfree (%)	18 / 21.9

The structure of Mn-Bound Structure of A TRICYT3 Variant also contains other interesting chemical elements:

Iron	(Fe)	3 atoms
Calcium	(Ca)	9 atoms
Chlorine	(Cl)	5 atoms

The binding sites of Manganese atom in the Mn-Bound Structure of A TRICYT3 Variant (pdb code 6wz7). 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 A TRICYT3 Variant, PDB code: 6wz7:

Manganese binding site 1 out of 1 in the Mn-Bound Structure of A TRICYT3 Variant


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 A TRICYT3 Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:31.4 occ:1.00 NE2 A:HIS73 2.2 28.8 1.0 NE2 B:HIS73 2.2 28.8 1.0 NE2 C:HIS73 2.2 28.4 1.0 NE2 C:HIS77 2.3 30.9 1.0 NE2 B:HIS77 2.3 32.0 1.0 NE2 A:HIS77 2.3 31.2 1.0 CE1 C:HIS77 3.0 30.0 1.0 CE1 B:HIS77 3.1 28.9 1.0 CE1 A:HIS77 3.1 28.8 1.0 CE1 B:HIS73 3.2 24.2 1.0 CE1 C:HIS73 3.2 25.7 1.0 CE1 A:HIS73 3.2 23.8 1.0 CD2 A:HIS73 3.2 21.5 1.0 CD2 B:HIS73 3.2 22.6 1.0 CD2 C:HIS73 3.3 22.1 1.0 CD2 C:HIS77 3.4 30.8 1.0 CD2 B:HIS77 3.4 33.1 1.0 CD2 A:HIS77 3.4 31.0 1.0 ND1 C:HIS77 4.2 29.1 1.0 ND1 B:HIS77 4.3 35.1 1.0 ND1 A:HIS77 4.3 29.5 1.0 ND1 B:HIS73 4.3 26.6 1.0 ND1 A:HIS73 4.3 24.2 1.0 ND1 C:HIS73 4.3 28.5 1.0 CG A:HIS73 4.3 23.8 1.0 CG B:HIS73 4.4 23.2 1.0 CG C:HIS73 4.4 22.4 1.0 CG C:HIS77 4.4 40.7 1.0 CG B:HIS77 4.5 41.5 1.0 CG A:HIS77 4.5 38.4 1.0 O B:HOH320 4.8 35.4 1.0 O A:HOH317 4.8 35.8 1.0 O C:HOH314 4.9 28.8 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