Iron in PDB 6wz0: Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2

The structure of Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2, PDB code: 6wz0 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)	47.78 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.206, 79.260, 49.916, 90.00, 106.89, 90.00
R / Rfree (%)	18.2 / 21.2

The binding sites of Iron atom in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2 (pdb code 6wz0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2, PDB code: 6wz0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:17.5 occ:1.00 FE A:HEC201 0.0 17.5 1.0 NB A:HEC201 2.0 15.3 1.0 NA A:HEC201 2.0 16.9 1.0 ND A:HEC201 2.0 15.3 1.0 NC A:HEC201 2.1 15.0 1.0 NE2 A:HIS102 2.1 17.7 1.0 SD A:MET7 2.4 18.4 1.0 C1B A:HEC201 3.0 19.0 1.0 C4A A:HEC201 3.0 18.8 1.0 C1A A:HEC201 3.0 17.5 1.0 C4D A:HEC201 3.0 20.7 1.0 C4B A:HEC201 3.0 16.7 1.0 C1D A:HEC201 3.1 17.1 1.0 C1C A:HEC201 3.1 16.7 1.0 CD2 A:HIS102 3.1 18.4 1.0 CE1 A:HIS102 3.1 19.0 1.0 C4C A:HEC201 3.1 16.3 1.0 CG A:MET7 3.4 16.5 1.0 CHB A:HEC201 3.4 17.8 1.0 CHA A:HEC201 3.4 20.0 1.0 CE A:MET7 3.4 21.6 1.0 CHC A:HEC201 3.4 18.4 1.0 CHD A:HEC201 3.5 19.1 1.0 CB A:MET7 4.2 16.5 1.0 ND1 A:HIS102 4.2 21.3 1.0 CG A:HIS102 4.2 19.7 1.0 C2A A:HEC201 4.2 16.5 1.0 C3A A:HEC201 4.2 19.1 1.0 C2B A:HEC201 4.2 18.9 1.0 C3B A:HEC201 4.3 15.9 1.0 C3D A:HEC201 4.3 18.6 1.0 C2D A:HEC201 4.3 19.3 1.0 C2C A:HEC201 4.3 15.3 1.0 C3C A:HEC201 4.3 17.5 1.0 NH1 A:ARG106 4.6 27.2 1.0 CA A:MET7 5.0 17.9 1.0

Iron binding site 2 out of 4 in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:14.9 occ:1.00 NE2 A:HIS73 2.2 17.9 1.0 NE2 B:HIS73 2.2 19.1 1.0 NE2 C:HIS73 2.2 19.1 1.0 NE2 C:HIS77 2.2 21.8 1.0 NE2 A:HIS77 2.2 19.4 1.0 NE2 B:HIS77 2.2 20.0 1.0 CD2 A:HIS77 3.1 22.7 1.0 CD2 C:HIS73 3.1 18.7 1.0 CD2 A:HIS73 3.1 15.6 1.0 CE1 C:HIS77 3.1 29.6 1.0 CD2 B:HIS73 3.1 17.5 1.0 CD2 C:HIS77 3.2 21.3 1.0 CE1 A:HIS73 3.2 20.9 1.0 CD2 B:HIS77 3.2 19.4 1.0 CE1 B:HIS73 3.2 22.1 1.0 CE1 B:HIS77 3.2 23.9 1.0 CE1 C:HIS73 3.2 19.7 1.0 CE1 A:HIS77 3.3 23.8 1.0 ND1 C:HIS77 4.2 29.8 1.0 CG A:HIS77 4.3 21.0 1.0 CG C:HIS73 4.3 19.2 1.0 CG C:HIS77 4.3 24.1 1.0 ND1 A:HIS73 4.3 19.0 1.0 ND1 B:HIS73 4.3 19.2 1.0 CG A:HIS73 4.3 17.1 1.0 ND1 C:HIS73 4.3 18.8 1.0 CG B:HIS73 4.3 13.9 1.0 ND1 B:HIS77 4.3 24.9 1.0 ND1 A:HIS77 4.3 25.5 1.0 CG B:HIS77 4.3 22.8 1.0 O A:HOH381 4.8 23.4 1.0 O C:HOH347 4.9 24.2 1.0 O B:HOH377 5.0 21.1 1.0

Iron binding site 3 out of 4 in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:21.3 occ:1.00 FE B:HEC201 0.0 21.3 1.0 NB B:HEC201 2.0 15.7 1.0 ND B:HEC201 2.0 14.1 1.0 NA B:HEC201 2.0 26.7 1.0 NC B:HEC201 2.0 21.2 1.0 NE2 B:HIS102 2.2 26.6 1.0 SD B:MET7 2.5 24.1 1.0 C1B B:HEC201 3.0 27.8 1.0 C4D B:HEC201 3.0 24.7 1.0 C4A B:HEC201 3.0 24.7 1.0 C4B B:HEC201 3.0 22.9 1.0 C4C B:HEC201 3.1 20.8 1.0 C1D B:HEC201 3.1 28.0 1.0 C1C B:HEC201 3.1 20.4 1.0 C1A B:HEC201 3.1 27.6 1.0 CD2 B:HIS102 3.1 21.5 1.0 CE1 B:HIS102 3.1 22.3 1.0 CHB B:HEC201 3.4 26.8 1.0 CHA B:HEC201 3.4 28.9 1.0 CHD B:HEC201 3.5 24.0 1.0 CHC B:HEC201 3.5 19.9 1.0 CE B:MET7 3.5 23.4 1.0 CG B:MET7 3.6 17.7 1.0 C2B B:HEC201 4.2 23.8 1.0 C3B B:HEC201 4.3 21.1 1.0 ND1 B:HIS102 4.3 29.8 1.0 C2D B:HEC201 4.3 25.2 1.0 C3D B:HEC201 4.3 26.1 1.0 C3A B:HEC201 4.3 30.0 1.0 CG B:HIS102 4.3 25.8 1.0 C3C B:HEC201 4.3 19.0 1.0 C2C B:HEC201 4.3 20.9 1.0 C2A B:HEC201 4.3 34.8 1.0 CB B:MET7 4.3 21.8 1.0

Iron binding site 4 out of 4 in the Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Fe-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:26.1 occ:1.00 FE C:HEC201 0.0 26.1 1.0 ND C:HEC201 2.0 24.6 1.0 NA C:HEC201 2.1 25.9 1.0 NB C:HEC201 2.1 23.4 1.0 NC C:HEC201 2.1 23.2 1.0 NE2 C:HIS102 2.3 30.1 1.0 SD C:MET7 2.5 24.5 1.0 C1D C:HEC201 3.0 25.2 1.0 C4D C:HEC201 3.0 27.5 1.0 C1A C:HEC201 3.1 30.7 1.0 C4C C:HEC201 3.1 22.5 1.0 C4B C:HEC201 3.1 28.6 1.0 C1C C:HEC201 3.1 24.7 1.0 C4A C:HEC201 3.1 26.9 1.0 C1B C:HEC201 3.1 28.8 1.0 CD2 C:HIS102 3.1 29.0 1.0 CE1 C:HIS102 3.4 34.4 1.0 CHA C:HEC201 3.4 31.9 1.0 CHD C:HEC201 3.4 25.4 1.0 CE C:MET7 3.4 29.6 1.0 CG C:MET7 3.4 23.0 1.0 CHC C:HEC201 3.5 28.4 1.0 CHB C:HEC201 3.5 30.3 1.0 C2D C:HEC201 4.2 27.4 1.0 C3D C:HEC201 4.2 28.3 1.0 CB C:MET7 4.2 24.6 1.0 C2A C:HEC201 4.3 31.8 1.0 C3C C:HEC201 4.3 23.1 1.0 C2C C:HEC201 4.3 23.6 1.0 C3A C:HEC201 4.3 26.7 1.0 C3B C:HEC201 4.3 27.8 1.0 C2B C:HEC201 4.3 28.7 1.0 CG C:HIS102 4.3 31.5 1.0 ND1 C:HIS102 4.4 28.3 1.0 NH2 C:ARG106 5.0 40.8 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