Iron 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:

Manganese	(Mn)	1 atom
Calcium	(Ca)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Iron 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 Iron atom.
In total 3 binding sites of Iron where determined in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz1:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe 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:Fe201 b:13.3 occ:1.00 FE A:HEC201 0.0 13.3 1.0 ND A:HEC201 2.0 15.0 1.0 NB A:HEC201 2.0 12.0 1.0 NC A:HEC201 2.1 13.8 1.0 NA A:HEC201 2.1 13.3 1.0 NE2 A:HIS102 2.2 13.3 1.0 SD A:MET7 2.4 11.8 1.0 C4D A:HEC201 3.1 13.3 1.0 C4B A:HEC201 3.1 10.7 1.0 C1A A:HEC201 3.1 15.3 1.0 C4A A:HEC201 3.1 13.3 1.0 C4C A:HEC201 3.1 12.2 1.0 C1D A:HEC201 3.1 13.0 1.0 C1B A:HEC201 3.1 15.2 1.0 C1C A:HEC201 3.1 14.3 1.0 CD2 A:HIS102 3.2 11.9 1.0 CE1 A:HIS102 3.2 13.7 1.0 CHA A:HEC201 3.4 14.1 1.0 CHD A:HEC201 3.4 13.7 1.0 CHC A:HEC201 3.5 13.2 1.0 CHB A:HEC201 3.5 11.7 1.0 CG A:MET7 3.5 12.3 1.0 CE A:MET7 3.5 13.3 1.0 C3B A:HEC201 4.3 11.3 1.0 C3D A:HEC201 4.3 17.6 1.0 C3A A:HEC201 4.3 17.4 1.0 C2A A:HEC201 4.3 16.2 1.0 C2D A:HEC201 4.3 13.4 1.0 C2B A:HEC201 4.3 8.6 1.0 C2C A:HEC201 4.3 11.6 1.0 C3C A:HEC201 4.3 14.4 1.0 ND1 A:HIS102 4.3 15.0 1.0 CB A:MET7 4.3 11.8 1.0 CG A:HIS102 4.3 12.7 1.0

Iron binding site 2 out of 3 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:14.5 occ:1.00 FE B:HEC201 0.0 14.5 1.0 NA B:HEC201 2.0 16.5 1.0 ND B:HEC201 2.0 12.4 1.0 NC B:HEC201 2.1 13.4 1.0 NB B:HEC201 2.1 15.1 1.0 NE2 B:HIS102 2.2 15.9 1.0 SD B:MET7 2.5 15.5 1.0 C1A B:HEC201 3.0 18.1 1.0 C1D B:HEC201 3.1 14.8 1.0 C4D B:HEC201 3.1 20.0 1.0 C1C B:HEC201 3.1 14.6 1.0 C4A B:HEC201 3.1 16.0 1.0 C4B B:HEC201 3.1 14.5 1.0 C1B B:HEC201 3.1 19.5 1.0 C4C B:HEC201 3.1 15.7 1.0 CD2 B:HIS102 3.1 13.9 1.0 CE1 B:HIS102 3.3 17.1 1.0 CHC B:HEC201 3.4 16.0 1.0 CHA B:HEC201 3.4 18.1 1.0 CHD B:HEC201 3.5 13.3 1.0 CHB B:HEC201 3.5 17.9 1.0 CE B:MET7 3.5 14.4 1.0 CG B:MET7 3.6 16.6 1.0 C2D B:HEC201 4.3 19.1 1.0 C2A B:HEC201 4.3 21.0 1.0 C3A B:HEC201 4.3 18.7 1.0 C3D B:HEC201 4.3 17.9 1.0 CB B:MET7 4.3 13.9 1.0 C2C B:HEC201 4.3 14.3 1.0 CG B:HIS102 4.3 17.8 1.0 C2B B:HEC201 4.3 18.6 1.0 ND1 B:HIS102 4.3 14.5 1.0 C3C B:HEC201 4.3 12.7 1.0 C3B B:HEC201 4.3 12.8 1.0

Iron binding site 3 out of 3 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:11.8 occ:1.00 FE C:HEC201 0.0 11.8 1.0 ND C:HEC201 2.0 11.9 1.0 NC C:HEC201 2.0 7.8 1.0 NB C:HEC201 2.0 9.2 1.0 NA C:HEC201 2.1 12.6 1.0 NE2 C:HIS102 2.2 12.7 1.0 SD C:MET7 2.5 11.1 1.0 C1D C:HEC201 3.0 11.8 1.0 C4D C:HEC201 3.0 13.6 1.0 C4B C:HEC201 3.0 12.2 1.0 C1C C:HEC201 3.0 15.6 1.0 C1A C:HEC201 3.1 15.2 1.0 C4C C:HEC201 3.1 13.5 1.0 C4A C:HEC201 3.1 13.2 1.0 C1B C:HEC201 3.1 11.9 1.0 CD2 C:HIS102 3.1 11.1 1.0 CE1 C:HIS102 3.1 14.9 1.0 CHC C:HEC201 3.4 12.2 1.0 CE C:MET7 3.4 15.3 1.0 CHA C:HEC201 3.4 15.1 1.0 CHD C:HEC201 3.4 10.4 1.0 CG C:MET7 3.4 16.7 1.0 CHB C:HEC201 3.5 10.9 1.0 C2D C:HEC201 4.2 14.2 1.0 C3D C:HEC201 4.2 13.3 1.0 ND1 C:HIS102 4.2 11.7 1.0 CG C:HIS102 4.3 11.3 1.0 C2C C:HEC201 4.3 13.0 1.0 C3B C:HEC201 4.3 10.1 1.0 C2A C:HEC201 4.3 12.6 1.0 C3C C:HEC201 4.3 9.2 1.0 C3A C:HEC201 4.3 14.5 1.0 C2B C:HEC201 4.3 14.1 1.0 CB C:MET7 4.3 18.2 1.0 NH1 C:ARG106 4.7 13.2 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