Iron in PDB 6etb: Aerobic S262Y Mutation of E. Coli Flrd Core

The structure of Aerobic S262Y Mutation of E. Coli Flrd Core, PDB code: 6etb was solved by P.T.Borges, C.V.Romao, M.A.Carrondo, M.Teixeira, C.Frazao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.76 / 1.91
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.383, 64.407, 147.254, 90.00, 91.09, 90.00
R / Rfree (%)	20 / 20

The binding sites of Iron atom in the Aerobic S262Y Mutation of E. Coli Flrd Core (pdb code 6etb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Aerobic S262Y Mutation of E. Coli Flrd Core, PDB code: 6etb:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:48.3 occ:1.00 O A:O505 1.7 29.7 0.6 NE2 A:HIS84 2.2 62.3 1.0 NE2 A:HIS227 2.2 23.2 1.0 OD2 A:ASP83 2.3 60.2 1.0 O2 A:OXY504 2.5 46.9 1.0 OD1 A:ASP166 2.7 28.6 1.0 CD2 A:HIS227 2.7 22.3 1.0 CE1 A:HIS84 2.9 63.0 1.0 O1 A:OXY504 3.3 47.8 1.0 CG A:ASP83 3.3 60.1 1.0 CD2 A:HIS84 3.3 61.3 1.0 CG A:ASP166 3.4 25.1 1.0 CE1 A:HIS227 3.5 23.9 1.0 FE A:FE503 3.6 38.9 1.0 OD2 A:ASP166 3.6 26.3 1.0 OD1 A:ASP83 3.6 59.4 1.0 OE1 A:GLU81 3.9 49.0 1.0 ND1 A:HIS84 4.0 62.7 1.0 CG A:HIS227 4.0 21.9 1.0 CG A:HIS84 4.3 61.5 1.0 ND1 A:HIS227 4.3 23.9 1.0 OG A:SER226 4.4 16.9 1.0 OH A:TYR194 4.4 30.2 1.0 O A:HOH607 4.5 50.2 0.7 CB A:ASP83 4.6 60.5 1.0 O A:HOH784 4.7 45.4 1.0 CB A:ASP166 4.8 20.9 1.0 CE1 A:HIS171 4.8 17.0 1.0 CD A:GLU81 4.9 47.5 1.0

Iron binding site 2 out of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:38.9 occ:1.00 OE1 A:GLU81 1.9 49.0 1.0 O A:O505 2.1 29.7 0.6 OD2 A:ASP166 2.2 26.3 1.0 O A:HOH628 2.5 53.0 1.0 NE2 A:HIS147 2.8 31.9 1.0 NE2 A:HIS79 2.9 29.2 1.0 CE1 A:HIS147 3.0 31.8 1.0 O A:HOH607 3.0 50.2 0.7 CD A:GLU81 3.0 47.5 1.0 O1 A:OXY504 3.1 47.8 1.0 CD2 A:HIS79 3.2 27.5 1.0 CG A:ASP166 3.3 25.1 1.0 O2 A:OXY504 3.5 46.9 1.0 FE A:FE502 3.6 48.3 1.0 OE2 A:GLU81 3.6 47.5 1.0 OD1 A:ASP166 3.8 28.6 1.0 CD2 A:HIS147 4.0 29.7 1.0 CE1 A:HIS79 4.1 28.9 1.0 NE2 A:HIS84 4.2 62.3 1.0 CG A:GLU81 4.2 46.1 1.0 CB A:GLU81 4.2 44.9 1.0 ND1 A:HIS147 4.2 30.1 1.0 CD2 A:HIS84 4.3 61.3 1.0 CB A:ASP166 4.5 20.9 1.0 OD1 A:ASP83 4.5 59.4 1.0 CG A:HIS79 4.6 25.4 1.0 OH A:TYR194 4.7 30.2 1.0 CG A:HIS147 4.8 28.4 1.0 O A:HOH791 4.8 30.9 1.0 OD2 A:ASP83 4.8 60.2 1.0 ND1 A:HIS79 5.0 26.4 1.0

Iron binding site 3 out of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:44.2 occ:1.00 O B:O505 1.7 36.3 0.6 NE2 B:HIS84 2.2 56.0 1.0 NE2 B:HIS227 2.2 22.7 1.0 OD2 B:ASP83 2.3 59.2 1.0 OD1 B:ASP166 2.5 28.5 1.0 O1 B:OXY504 2.7 51.1 1.0 CD2 B:HIS227 2.7 23.9 1.0 CE1 B:HIS84 2.7 57.4 1.0 CG B:ASP83 3.3 58.1 1.0 CG B:ASP166 3.3 25.9 1.0 O2 B:OXY504 3.3 55.1 1.0 CD2 B:HIS84 3.4 55.8 1.0 O B:HOH660 3.5 48.4 1.0 CE1 B:HIS227 3.5 23.7 1.0 OD2 B:ASP166 3.5 26.5 1.0 FE B:FE503 3.6 40.1 1.0 OD1 B:ASP83 3.7 56.9 1.0 ND1 B:HIS84 3.9 58.0 1.0 CG B:HIS227 4.0 23.6 1.0 OE1 B:GLU81 4.1 51.6 1.0 CG B:HIS84 4.3 57.7 1.0 OG B:SER226 4.3 17.9 1.0 ND1 B:HIS227 4.3 24.6 1.0 OH B:TYR194 4.4 29.6 1.0 CB B:ASP83 4.6 58.3 1.0 CB B:ASP166 4.7 23.8 1.0 O B:HOH604 4.9 47.6 1.0 CE1 B:HIS171 4.9 18.4 1.0 CD B:GLU81 5.0 49.5 1.0

Iron binding site 4 out of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe503 b:40.1 occ:1.00 OE1 B:GLU81 1.9 51.6 1.0 O B:O505 2.1 36.3 0.6 OD2 B:ASP166 2.1 26.5 1.0 NE2 B:HIS147 2.6 39.6 1.0 NE2 B:HIS79 2.7 30.8 1.0 CE1 B:HIS147 2.7 38.7 1.0 CD B:GLU81 3.1 49.5 1.0 CD2 B:HIS79 3.1 29.4 1.0 O2 B:OXY504 3.1 55.1 1.0 CG B:ASP166 3.2 25.9 1.0 O B:HOH604 3.2 47.6 1.0 FE B:FE502 3.6 44.2 1.0 OE2 B:GLU81 3.7 49.6 1.0 OD1 B:ASP166 3.7 28.5 1.0 O1 B:OXY504 3.7 51.1 1.0 CD2 B:HIS147 3.9 38.7 1.0 CE1 B:HIS79 3.9 29.6 1.0 ND1 B:HIS147 4.0 36.9 1.0 NE2 B:HIS84 4.0 56.0 1.0 CB B:GLU81 4.2 44.7 1.0 CG B:GLU81 4.2 46.8 1.0 CD2 B:HIS84 4.2 55.8 1.0 CB B:ASP166 4.4 23.8 1.0 CG B:HIS79 4.4 27.6 1.0 OD1 B:ASP83 4.6 56.9 1.0 CG B:HIS147 4.6 36.6 1.0 O B:HOH613 4.6 46.8 1.0 OH B:TYR194 4.7 29.6 1.0 O B:HOH660 4.8 48.4 1.0 ND1 B:HIS79 4.8 27.4 1.0 OD2 B:ASP83 4.8 59.2 1.0

P.T.Borges, C.V.Romao, M.A.Carrondo, M.Teixeira, C.Frazao. A Tyrosine Mutation in E. Coli Flavodiiron Protein Increases Radiation Sensitivity in the Crystal Structure To Be Published.