Iron in PDB 6wz2: Co-Bound Structure of An Engineered Protein Trimer, TRICYT3

The structure of Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz2 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)	35.05 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.252, 78.105, 49.562, 90.00, 106.64, 90.00
R / Rfree (%)	17.5 / 21.8

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

Cobalt	(Co)	1 atom
Chlorine	(Cl)	5 atoms

The binding sites of Iron atom in the Co-Bound Structure of An Engineered Protein Trimer, TRICYT3 (pdb code 6wz2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Co-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz2:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Co-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 Co-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:16.7 occ:1.00 FE A:HEC201 0.0 16.7 1.0 NA A:HEC201 2.0 15.3 1.0 ND A:HEC201 2.0 15.6 1.0 NC A:HEC201 2.1 12.9 1.0 NB A:HEC201 2.1 16.3 1.0 NE2 A:HIS102 2.2 19.1 1.0 SD A:MET7 2.4 16.4 1.0 C4A A:HEC201 3.0 20.3 1.0 C1A A:HEC201 3.0 16.9 1.0 C1D A:HEC201 3.1 19.4 1.0 C4C A:HEC201 3.1 16.6 1.0 C4D A:HEC201 3.1 17.0 1.0 C1C A:HEC201 3.1 18.9 1.0 C4B A:HEC201 3.1 19.1 1.0 C1B A:HEC201 3.1 19.2 1.0 CE1 A:HIS102 3.1 21.1 1.0 CD2 A:HIS102 3.2 15.3 1.0 CHD A:HEC201 3.4 14.6 1.0 CHA A:HEC201 3.4 17.0 1.0 CHB A:HEC201 3.4 15.5 1.0 CHC A:HEC201 3.5 17.6 1.0 CE A:MET7 3.5 18.0 1.0 CG A:MET7 3.5 16.4 1.0 ND1 A:HIS102 4.2 18.1 1.0 C2A A:HEC201 4.3 18.3 1.0 C3A A:HEC201 4.3 18.7 1.0 C2D A:HEC201 4.3 16.6 1.0 C3D A:HEC201 4.3 17.7 1.0 C3C A:HEC201 4.3 17.4 1.0 CG A:HIS102 4.3 19.2 1.0 C2C A:HEC201 4.3 15.8 1.0 CB A:MET7 4.3 17.4 1.0 C3B A:HEC201 4.3 18.2 1.0 C2B A:HEC201 4.3 19.2 1.0

Iron binding site 2 out of 3 in the Co-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 Co-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:21.1 occ:1.00 FE B:HEC201 0.0 21.1 1.0 NC B:HEC201 2.0 18.9 1.0 ND B:HEC201 2.0 21.6 1.0 NB B:HEC201 2.1 16.9 1.0 NA B:HEC201 2.1 25.6 1.0 NE2 B:HIS102 2.2 23.8 1.0 SD B:MET7 2.4 21.6 1.0 C1C B:HEC201 3.0 19.6 1.0 C4B B:HEC201 3.1 20.2 1.0 C4D B:HEC201 3.1 26.5 1.0 C1D B:HEC201 3.1 24.6 1.0 C1A B:HEC201 3.1 25.0 1.0 C4C B:HEC201 3.1 20.9 1.0 C1B B:HEC201 3.1 19.0 1.0 CD2 B:HIS102 3.1 22.9 1.0 C4A B:HEC201 3.1 27.6 1.0 CE1 B:HIS102 3.2 26.5 1.0 CHC B:HEC201 3.4 19.9 1.0 CHA B:HEC201 3.4 23.8 1.0 CE B:MET7 3.4 16.2 1.0 CHD B:HEC201 3.5 21.2 1.0 CG B:MET7 3.5 18.4 1.0 CHB B:HEC201 3.5 20.7 1.0 C2C B:HEC201 4.3 22.0 1.0 CB B:MET7 4.3 20.9 1.0 C2D B:HEC201 4.3 21.6 1.0 C3D B:HEC201 4.3 27.4 1.0 C3C B:HEC201 4.3 22.0 1.0 C2A B:HEC201 4.3 25.5 1.0 C3B B:HEC201 4.3 19.6 1.0 CG B:HIS102 4.3 25.2 1.0 ND1 B:HIS102 4.3 26.4 1.0 C2B B:HEC201 4.3 20.2 1.0 C3A B:HEC201 4.3 25.1 1.0

Iron binding site 3 out of 3 in the Co-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 Co-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:16.9 occ:1.00 FE C:HEC201 0.0 16.9 1.0 NA C:HEC201 2.0 17.9 1.0 ND C:HEC201 2.0 13.4 1.0 NC C:HEC201 2.0 15.8 1.0 NB C:HEC201 2.1 10.7 1.0 NE2 C:HIS102 2.2 15.3 1.0 SD C:MET7 2.4 16.2 1.0 C1D C:HEC201 3.0 17.3 1.0 C1A C:HEC201 3.0 16.5 1.0 C4C C:HEC201 3.1 15.5 1.0 C4D C:HEC201 3.1 18.8 1.0 C4A C:HEC201 3.1 15.8 1.0 C1C C:HEC201 3.1 16.5 1.0 C1B C:HEC201 3.1 15.0 1.0 CD2 C:HIS102 3.1 16.5 1.0 C4B C:HEC201 3.1 14.3 1.0 CE1 C:HIS102 3.2 18.1 1.0 CHD C:HEC201 3.4 15.6 1.0 CHA C:HEC201 3.4 19.3 1.0 CG C:MET7 3.4 19.0 1.0 CHB C:HEC201 3.4 13.0 1.0 CE C:MET7 3.5 12.8 1.0 CHC C:HEC201 3.5 14.7 1.0 CB C:MET7 4.2 16.6 1.0 C2A C:HEC201 4.3 20.7 1.0 C2D C:HEC201 4.3 18.0 1.0 C3A C:HEC201 4.3 16.5 1.0 C3D C:HEC201 4.3 18.0 1.0 CG C:HIS102 4.3 18.8 1.0 C3C C:HEC201 4.3 14.2 1.0 ND1 C:HIS102 4.3 17.8 1.0 C2C C:HEC201 4.3 14.2 1.0 C2B C:HEC201 4.3 15.6 1.0 C3B C:HEC201 4.3 13.9 1.0 NH1 C:ARG106 4.7 16.3 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