Iron in PDB 7lra: Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2)

The structure of Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2), PDB code: 7lra 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)	41.65 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.76, 61, 64.16, 90, 90, 90
R / Rfree (%)	18 / 21.4

The structure of Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2) also contains other interesting chemical elements:

Nickel

(Ni)

2 atoms

The binding sites of Iron atom in the Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2) (pdb code 7lra). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2), PDB code: 7lra:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:15.0 occ:1.00 FE C:HEC201 0.0 15.0 1.0 NA C:HEC201 2.0 13.8 1.0 NC C:HEC201 2.0 13.8 1.0 ND C:HEC201 2.0 12.1 1.0 NB C:HEC201 2.0 12.9 1.0 NE2 C:HIS102 2.1 15.6 1.0 SD C:MET7 2.4 13.5 1.0 C1A C:HEC201 3.0 13.8 1.0 C4A C:HEC201 3.0 13.9 1.0 C1B C:HEC201 3.0 12.2 1.0 C1C C:HEC201 3.1 15.1 1.0 C4D C:HEC201 3.1 15.0 1.0 CD2 C:HIS102 3.1 14.3 1.0 C1D C:HEC201 3.1 14.4 1.0 C4B C:HEC201 3.1 16.0 1.0 C4C C:HEC201 3.1 15.7 1.0 CE1 C:HIS102 3.2 15.2 1.0 CHB C:HEC201 3.4 13.2 1.0 CHA C:HEC201 3.4 14.8 1.0 CE C:MET7 3.4 12.9 1.0 CG C:MET7 3.4 11.8 1.0 CHC C:HEC201 3.4 15.8 1.0 CHD C:HEC201 3.4 15.9 1.0 CB C:MET7 4.2 14.7 1.0 C2A C:HEC201 4.2 16.0 1.0 CG C:HIS102 4.2 14.8 1.0 C3A C:HEC201 4.2 14.0 1.0 ND1 C:HIS102 4.2 13.6 1.0 C2B C:HEC201 4.3 12.9 1.0 C2C C:HEC201 4.3 19.5 1.0 C3B C:HEC201 4.3 13.7 1.0 C2D C:HEC201 4.3 14.3 1.0 C3D C:HEC201 4.3 15.8 1.0 C3C C:HEC201 4.3 20.3 1.0 CA C:MET7 5.0 13.4 1.0

Iron binding site 2 out of 2 in the Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ni-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (M1) and Ni(II) (M2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:20.0 occ:1.00 FE A:HEC201 0.0 20.0 1.0 ND A:HEC201 2.0 18.0 1.0 NB A:HEC201 2.0 16.9 1.0 NC A:HEC201 2.0 18.3 1.0 NA A:HEC201 2.1 16.3 1.0 NE2 A:HIS102 2.2 22.0 1.0 SD A:MET7 2.5 18.7 1.0 C1D A:HEC201 3.0 22.0 1.0 C4D A:HEC201 3.0 23.2 1.0 C4B A:HEC201 3.1 16.3 1.0 C1C A:HEC201 3.1 18.4 1.0 C1B A:HEC201 3.1 18.7 1.0 C1A A:HEC201 3.1 22.5 1.0 C4C A:HEC201 3.1 20.1 1.0 C4A A:HEC201 3.1 20.2 1.0 CD2 A:HIS102 3.1 18.1 1.0 CE1 A:HIS102 3.2 21.4 1.0 CHD A:HEC201 3.4 23.2 1.0 CHA A:HEC201 3.4 23.8 1.0 CHC A:HEC201 3.4 16.0 1.0 CHB A:HEC201 3.4 22.1 1.0 CE A:MET7 3.5 20.1 1.0 CG A:MET7 3.6 18.5 1.0 C2D A:HEC201 4.3 22.6 1.0 C3D A:HEC201 4.3 25.4 1.0 CB A:MET7 4.3 17.7 1.0 C3B A:HEC201 4.3 17.4 1.0 C2B A:HEC201 4.3 17.0 1.0 C2C A:HEC201 4.3 16.0 1.0 ND1 A:HIS102 4.3 20.4 1.0 C2A A:HEC201 4.3 22.8 1.0 C3A A:HEC201 4.3 21.2 1.0 C3C A:HEC201 4.3 17.6 1.0 CG A:HIS102 4.3 19.4 1.0 NH1 A:ARG106 4.6 35.1 1.0

T.S.Choi, F.A.Tezcan. Structure-Guided Metal Selectivity in Malleable Protein Interface Mediated By Single Disulfide Bond To Be Published.