Iron in PDB 7n4g: Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II)

The structure of Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II), PDB code: 7n4g was solved by T.S.Choi, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.60 / 1.93
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.21, 78.27, 39, 90, 100.68, 90
R / Rfree (%)	26.4 / 32.5

The structure of Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II) also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Iron atom in the Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II) (pdb code 7n4g). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II), PDB code: 7n4g:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:53.5 occ:1.00 FE C:HEC201 0.0 53.5 1.0 NC C:HEC201 2.0 44.9 1.0 NB C:HEC201 2.1 47.8 1.0 NA C:HEC201 2.1 50.5 1.0 ND C:HEC201 2.1 45.5 1.0 NE2 C:HIS102 2.3 33.8 1.0 SD C:MET7 2.6 42.5 1.0 C1C C:HEC201 3.0 41.7 1.0 C4B C:HEC201 3.0 40.4 1.0 C4D C:HEC201 3.0 46.5 1.0 C1A C:HEC201 3.0 42.6 1.0 C1D C:HEC201 3.1 39.0 1.0 C4C C:HEC201 3.1 43.8 1.0 C1B C:HEC201 3.1 42.4 1.0 C4A C:HEC201 3.1 48.7 1.0 CD2 C:HIS102 3.2 36.3 1.0 CE1 C:HIS102 3.3 39.4 1.0 CHC C:HEC201 3.3 37.6 1.0 CHA C:HEC201 3.4 44.4 1.0 CG C:MET7 3.5 41.5 1.0 CHB C:HEC201 3.5 47.7 1.0 CHD C:HEC201 3.5 44.0 1.0 CE C:MET7 3.6 40.0 1.0 CB C:MET7 3.9 41.5 1.0 C2C C:HEC201 4.2 39.8 1.0 C3D C:HEC201 4.2 45.7 1.0 C2A C:HEC201 4.3 45.4 1.0 C3B C:HEC201 4.3 36.7 1.0 C2D C:HEC201 4.3 48.8 1.0 C3C C:HEC201 4.3 36.8 1.0 C3A C:HEC201 4.3 48.4 1.0 C2B C:HEC201 4.3 39.3 1.0 ND1 C:HIS102 4.4 36.1 1.0 CG C:HIS102 4.4 35.3 1.0 CA C:MET7 4.9 42.5 1.0

Iron binding site 2 out of 2 in the Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Co-Bound Crystal Structure of the Engineered Cyt CB562 Variant, AB2- H100A, Crystallized in the Presence of Co(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:57.7 occ:1.00 FE A:HEC201 0.0 57.7 1.0 ND A:HEC201 2.0 49.2 1.0 NB A:HEC201 2.0 47.3 1.0 NA A:HEC201 2.0 51.6 1.0 NC A:HEC201 2.1 43.7 1.0 NE2 A:HIS102 2.5 38.4 1.0 SD A:MET7 2.7 49.9 1.0 C4D A:HEC201 2.9 52.3 1.0 C1A A:HEC201 3.0 53.3 1.0 C4B A:HEC201 3.0 42.7 1.0 C1C A:HEC201 3.0 40.3 1.0 CD2 A:HIS102 3.0 41.9 1.0 C1D A:HEC201 3.1 51.9 1.0 C1B A:HEC201 3.1 44.7 1.0 C4A A:HEC201 3.1 48.6 1.0 C4C A:HEC201 3.2 44.8 1.0 CHA A:HEC201 3.3 49.9 1.0 CHC A:HEC201 3.3 40.1 1.0 CG A:MET7 3.4 55.6 1.0 CHB A:HEC201 3.5 52.1 1.0 CHD A:HEC201 3.5 44.1 1.0 CE A:MET7 3.6 51.0 1.0 CE1 A:HIS102 3.7 43.4 1.0 C3D A:HEC201 4.2 51.8 1.0 C2A A:HEC201 4.2 55.2 1.0 CB A:MET7 4.2 56.3 1.0 C3B A:HEC201 4.2 38.3 1.0 C2D A:HEC201 4.2 51.9 1.0 C2B A:HEC201 4.3 41.0 1.0 C3A A:HEC201 4.3 54.0 1.0 C2C A:HEC201 4.3 44.4 1.0 CG A:HIS102 4.3 41.7 1.0 C3C A:HEC201 4.4 40.9 1.0 ND1 A:HIS102 4.6 44.0 1.0 CA A:MET7 5.0 56.5 1.0

T.S.Choi, F.A.Tezcan. Overcoming Universal Restrictions on Metal Selectivity By Protein Design. Nature V. 603 522 2022.
ISSN: ESSN 1476-4687
PubMed: 35236987
DOI: 10.1038/S41586-022-04469-8