Iron in PDB 3ogh: Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins

The structure of Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins, PDB code: 3ogh was solved by B.Nocek, L.Bigelow, J.Bearden, A.Joachimiak, Midwest Center Forstructural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	30.148, 90.295, 58.132, 90.00, 103.51, 90.00
R / Rfree (%)	16.6 / 21.3

The structure of Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Iron atom in the Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins (pdb code 3ogh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins, PDB code: 3ogh:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:11.2 occ:0.80 OE1 B:GLU107 2.0 20.9 1.0 OE1 B:GLU104 2.0 25.8 1.0 OE1 B:GLU137 2.1 21.1 1.0 NE2 B:HIS45 2.1 21.1 1.0 O B:HOH173 2.2 22.5 1.0 O B:HOH174 2.5 30.4 1.0 CD B:GLU104 2.8 21.5 1.0 OE2 B:GLU104 2.8 32.8 1.0 CD B:GLU137 3.0 20.1 1.0 CD B:GLU107 3.1 20.9 1.0 CE1 B:HIS45 3.1 21.1 1.0 CD2 B:HIS45 3.2 20.9 1.0 OE2 B:GLU137 3.4 20.7 1.0 OE2 B:GLU107 3.4 21.1 1.0 MG B:MG501 3.5 7.8 0.9 CG B:GLU137 4.2 19.8 1.0 ND1 B:HIS45 4.3 21.1 1.0 CG B:GLU104 4.3 20.9 1.0 CG B:HIS45 4.3 20.9 1.0 OG1 B:THR49 4.4 20.7 1.0 CB B:GLU137 4.4 19.6 1.0 CG B:GLU107 4.4 20.6 1.0 OE1 B:GLN52 4.5 20.8 1.0 CA B:GLU137 4.5 19.4 1.0 NE2 B:GLN52 4.6 21.1 1.0 CA B:GLU104 4.8 20.5 1.0 CB B:GLU104 4.8 20.6 1.0 CB B:GLU107 4.9 20.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:21.5 occ:0.80 OE1 A:GLU107 2.0 28.2 1.0 OE1 A:GLU137 2.0 29.2 1.0 O A:HOH169 2.1 25.8 1.0 NE2 A:HIS45 2.2 30.1 1.0 OE1 A:GLU104 2.2 34.0 1.0 O A:HOH170 2.5 31.9 1.0 CD A:GLU104 2.9 30.1 1.0 CD A:GLU137 3.0 25.9 1.0 OE2 A:GLU104 3.0 37.4 1.0 CD A:GLU107 3.1 24.0 1.0 CD2 A:HIS45 3.1 29.1 1.0 CE1 A:HIS45 3.2 30.6 1.0 OE2 A:GLU137 3.4 28.1 1.0 MG A:MG501 3.5 18.2 1.0 OE2 A:GLU107 3.5 26.3 1.0 ND1 A:HIS45 4.3 31.1 1.0 CG A:GLU137 4.3 24.5 1.0 OG1 A:THR49 4.3 29.4 1.0 CG A:HIS45 4.3 29.6 1.0 CG A:GLU107 4.4 23.1 1.0 CG A:GLU104 4.4 25.8 1.0 OE1 A:GLN52 4.5 31.4 1.0 CB A:GLU137 4.5 23.6 1.0 CA A:GLU137 4.6 23.9 1.0 NE2 A:GLN52 4.7 29.8 1.0 CA A:GLU104 4.8 22.4 1.0 CB A:GLU107 4.8 22.0 1.0 CB A:GLU104 4.9 23.4 1.0

B.Nocek, L.Bigelow, J.Bearden, A.Joachimiak. Crystal Structure of Ycie Protein From E. Coli CFT073, A Member of Ferritine-Like Superfamily of Diiron-Containing Four-Helix-Bundle Proteins To Be Published.