Iron in PDB 7lv4: Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II)

The structure of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II), PDB code: 7lv4 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)	33.38 / 1.99
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.964, 83.927, 38.541, 90, 100.67, 90
R / Rfree (%)	24 / 30.6

The structure of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II) also contains other interesting chemical elements:

Calcium	(Ca)	3 atoms
Copper	(Cu)	1 atom

The binding sites of Iron atom in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II) (pdb code 7lv4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II), PDB code: 7lv4:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:26.4 occ:1.00 FE C:HEC201 0.0 26.4 1.0 NB C:HEC201 2.0 26.1 1.0 ND C:HEC201 2.0 24.6 1.0 NC C:HEC201 2.0 23.3 1.0 NA C:HEC201 2.1 27.3 1.0 NE2 C:HIS102 2.3 23.9 1.0 SD C:MET7 2.6 21.8 1.0 C4B C:HEC201 3.0 20.9 1.0 C1C C:HEC201 3.0 23.2 1.0 C4D C:HEC201 3.0 25.2 1.0 C1A C:HEC201 3.1 27.3 1.0 C1D C:HEC201 3.1 26.4 1.0 C1B C:HEC201 3.1 23.0 1.0 C4C C:HEC201 3.1 22.3 1.0 CD2 C:HIS102 3.1 20.8 1.0 C4A C:HEC201 3.2 24.6 1.0 CE1 C:HIS102 3.3 20.4 1.0 CHC C:HEC201 3.3 20.1 1.0 CHA C:HEC201 3.4 25.0 1.0 CE C:MET7 3.4 21.1 1.0 CHD C:HEC201 3.5 27.3 1.0 CHB C:HEC201 3.5 19.7 1.0 CG C:MET7 3.6 28.8 1.0 C3B C:HEC201 4.2 26.2 1.0 C2C C:HEC201 4.2 25.2 1.0 C3D C:HEC201 4.3 24.5 1.0 C2B C:HEC201 4.3 23.2 1.0 C2D C:HEC201 4.3 31.0 1.0 C3C C:HEC201 4.3 25.6 1.0 CG C:HIS102 4.3 24.3 1.0 C2A C:HEC201 4.3 32.4 1.0 CB C:MET7 4.3 16.6 1.0 ND1 C:HIS102 4.4 22.0 1.0 C3A C:HEC201 4.4 21.4 1.0

Iron binding site 2 out of 2 in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2 - H97A, Crystallized in the Presence of Cu(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:27.7 occ:1.00 FE A:HEC201 0.0 27.7 1.0 ND A:HEC201 2.0 20.5 1.0 NA A:HEC201 2.0 25.7 1.0 NB A:HEC201 2.1 26.8 1.0 NC A:HEC201 2.1 20.1 1.0 NE2 A:HIS102 2.3 28.4 1.0 SD A:MET7 2.5 21.1 1.0 C4D A:HEC201 3.0 25.6 1.0 C1A A:HEC201 3.0 23.7 1.0 C1D A:HEC201 3.0 22.6 1.0 C4A A:HEC201 3.0 29.0 1.0 C1C A:HEC201 3.1 24.1 1.0 C4B A:HEC201 3.1 27.2 1.0 C1B A:HEC201 3.1 23.3 1.0 C4C A:HEC201 3.1 19.0 1.0 CE1 A:HIS102 3.2 28.0 1.0 CD2 A:HIS102 3.2 23.1 1.0 CHA A:HEC201 3.4 24.2 1.0 CE A:MET7 3.4 26.4 1.0 CG A:MET7 3.4 27.4 1.0 CHD A:HEC201 3.4 30.7 1.0 CHB A:HEC201 3.4 28.4 1.0 CHC A:HEC201 3.5 20.7 1.0 CB A:MET7 4.2 27.9 1.0 C2D A:HEC201 4.2 33.7 1.0 C3D A:HEC201 4.2 29.2 1.0 C2A A:HEC201 4.2 26.9 1.0 C3A A:HEC201 4.2 25.9 1.0 C2B A:HEC201 4.3 25.5 1.0 C2C A:HEC201 4.3 19.5 1.0 C3B A:HEC201 4.3 18.7 1.0 C3C A:HEC201 4.3 28.2 1.0 ND1 A:HIS102 4.4 33.1 1.0 CG A:HIS102 4.4 30.1 1.0 CA A:MET7 5.0 28.6 1.0

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