Iron in PDB 2htn: E. Coli Bacterioferritin in Its As-Isolated Form

All present enzymatic activity of E. Coli Bacterioferritin in Its As-Isolated Form:
1.16.3.1;

The structure of E. Coli Bacterioferritin in Its As-Isolated Form, PDB code: 2htn was solved by A.Van Eerde, S.Wolterink-Van Loo, J.Van Der Oost, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.34 / 2.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	167.893, 167.893, 167.893, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 18.8

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Iron atom in the E. Coli Bacterioferritin in Its As-Isolated Form (pdb code 2htn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the E. Coli Bacterioferritin in Its As-Isolated Form, PDB code: 2htn:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:23.6 occ:1.00 OE2 A:GLU127 1.9 34.8 1.0 ND1 A:HIS54 2.1 13.6 1.0 OE2 A:GLU18 2.1 34.4 1.0 OE1 A:GLU51 2.3 30.9 1.0 OE1 A:GLU18 2.3 49.1 1.0 CD A:GLU18 2.5 23.9 1.0 CD A:GLU127 2.9 15.9 1.0 CE1 A:HIS54 3.0 24.6 1.0 CG A:HIS54 3.1 10.5 1.0 CD A:GLU51 3.2 12.4 1.0 OE1 A:GLU127 3.2 29.0 1.0 OE2 A:GLU51 3.4 45.2 1.0 CB A:HIS54 3.4 18.7 1.0 FE A:FE302 3.9 44.2 0.8 CG A:GLU18 4.0 32.8 1.0 CG2 A:ILE123 4.1 10.2 1.0 NE2 A:HIS54 4.2 25.7 1.0 CG A:GLU127 4.2 26.8 1.0 CD2 A:HIS54 4.2 25.6 1.0 CA A:GLU51 4.2 17.6 1.0 CG A:GLU51 4.4 29.2 1.0 CB A:GLU51 4.7 9.3 1.0 CE1 A:HIS130 4.8 60.1 1.0 CB A:GLU18 4.9 23.1 1.0 N A:GLU51 4.9 14.2 1.0 O A:ASP50 4.9 17.2 1.0 O A:GLU51 4.9 17.0 1.0 CA A:HIS54 5.0 15.2 1.0

Iron binding site 2 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe302 b:44.2 occ:0.75 OE1 A:GLU127 2.0 29.0 1.0 OE1 A:GLU94 2.1 42.1 1.0 OE2 A:GLU51 2.2 45.2 1.0 ND1 A:HIS130 2.4 40.8 1.0 CD A:GLU94 2.7 35.8 1.0 OE2 A:GLU94 2.8 47.4 1.0 CD A:GLU51 3.0 12.4 1.0 CD A:GLU127 3.1 15.9 1.0 CE1 A:HIS130 3.1 60.1 1.0 OE1 A:GLU51 3.3 30.9 1.0 OE2 A:GLU127 3.5 34.8 1.0 CG A:HIS130 3.5 47.9 1.0 FE A:FE301 3.9 23.6 1.0 CB A:HIS130 4.0 23.2 1.0 CG A:GLU94 4.1 34.9 1.0 OH A:TYR25 4.2 46.7 1.0 CE2 A:TYR25 4.3 30.6 1.0 CG A:GLU127 4.3 26.8 1.0 NE2 A:HIS130 4.3 43.4 1.0 CA A:GLU127 4.3 15.0 1.0 CG A:GLU51 4.3 29.2 1.0 CB A:GLU127 4.4 10.6 1.0 CD2 A:HIS130 4.5 58.5 1.0 CZ A:TYR25 4.7 53.2 1.0 OE1 A:GLU18 4.9 49.1 1.0 CB A:GLU94 5.0 17.8 1.0 O A:GLU127 5.0 19.7 1.0

Iron binding site 3 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:23.0 occ:1.00 FE A:HEM200 0.0 23.0 1.0 NA A:HEM200 2.0 9.5 0.5 ND A:HEM200 2.0 11.3 0.5 ND A:HEM200 2.1 29.6 0.5 NC A:HEM200 2.1 40.9 0.5 NB A:HEM200 2.1 42.4 0.5 NA A:HEM200 2.1 26.7 0.5 NC A:HEM200 2.1 2.0 0.5 NB A:HEM200 2.1 20.7 0.5 SD A:MET52 2.3 15.1 1.0 SD B:MET52 2.4 17.0 1.0 C4D A:HEM200 3.0 13.2 0.5 C1A A:HEM200 3.0 13.9 0.5 C1D A:HEM200 3.0 3.6 0.5 C1D A:HEM200 3.0 48.7 0.5 C4C A:HEM200 3.1 51.2 0.5 C4A A:HEM200 3.1 6.6 0.5 C4D A:HEM200 3.1 35.0 0.5 C1B A:HEM200 3.1 38.7 0.5 C4C A:HEM200 3.1 19.7 0.5 C4A A:HEM200 3.1 20.4 0.5 C1A A:HEM200 3.1 30.4 0.5 C4B A:HEM200 3.1 55.8 0.5 C1B A:HEM200 3.1 13.5 0.5 C1C A:HEM200 3.1 52.4 0.5 C1C A:HEM200 3.2 2.0 0.5 C4B A:HEM200 3.2 2.0 0.5 CHA A:HEM200 3.3 3.6 0.5 CG A:MET52 3.4 11.1 1.0 CHD A:HEM200 3.4 54.4 0.5 CE A:MET52 3.4 10.7 1.0 CHD A:HEM200 3.4 2.0 0.5 CE B:MET52 3.4 10.6 1.0 CHB A:HEM200 3.4 6.5 0.5 CHA A:HEM200 3.5 24.3 0.5 CHB A:HEM200 3.5 47.8 0.5 CHC A:HEM200 3.5 56.7 0.5 CG B:MET52 3.5 11.2 1.0 CHC A:HEM200 3.6 8.6 0.5 CB A:MET52 4.1 15.3 1.0 C3D A:HEM200 4.2 6.0 0.5 C2A A:HEM200 4.2 23.8 0.5 C2D A:HEM200 4.2 4.7 0.5 C3A A:HEM200 4.3 7.0 0.5 C3C A:HEM200 4.3 43.1 0.5 CB B:MET52 4.3 15.2 1.0 C2D A:HEM200 4.3 38.3 0.5 C3D A:HEM200 4.3 57.3 0.5 C2B A:HEM200 4.3 59.1 0.5 C3B A:HEM200 4.3 76.8 0.5 C2C A:HEM200 4.3 48.6 0.5 C2A A:HEM200 4.3 34.3 0.5 C3A A:HEM200 4.3 46.7 0.5 C3C A:HEM200 4.3 19.9 0.5 C2B A:HEM200 4.4 2.0 0.5 C2C A:HEM200 4.4 4.9 0.5 C3B A:HEM200 4.4 24.8 0.5

Iron binding site 4 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:30.7 occ:1.00 OE2 B:GLU127 1.9 66.9 1.0 OE2 B:GLU18 2.2 34.5 1.0 ND1 B:HIS54 2.2 12.0 1.0 OE1 B:GLU51 2.3 25.5 1.0 OE1 B:GLU18 2.3 43.5 1.0 CD B:GLU18 2.6 16.8 1.0 CD B:GLU127 2.8 2.0 1.0 OE1 B:GLU127 3.0 54.0 1.0 CE1 B:HIS54 3.1 16.6 1.0 CD B:GLU51 3.1 5.3 1.0 CG B:HIS54 3.2 9.7 1.0 OE2 B:GLU51 3.5 19.2 1.0 CB B:HIS54 3.5 22.3 1.0 FE B:FE302 3.6 47.4 0.8 CG B:GLU18 4.0 25.0 1.0 CG B:GLU127 4.1 53.7 1.0 CG2 B:ILE123 4.1 7.0 1.0 CA B:GLU51 4.1 22.0 1.0 NE2 B:HIS54 4.2 13.0 1.0 CD2 B:HIS54 4.3 34.6 1.0 CG B:GLU51 4.3 24.8 1.0 CB B:GLU51 4.5 20.0 1.0 CE1 B:HIS130 4.5 76.6 1.0 N B:GLU51 4.8 13.0 1.0 O B:ASP50 4.9 14.2 1.0 ND1 B:HIS130 4.9 24.9 1.0

Iron binding site 5 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe302 b:47.4 occ:0.75 OE1 B:GLU127 1.7 54.0 1.0 OE2 B:GLU94 2.1 22.8 1.0 OE2 B:GLU51 2.2 19.2 1.0 ND1 B:HIS130 2.5 24.9 1.0 OE1 B:GLU94 2.6 38.7 1.0 CD B:GLU94 2.7 33.1 1.0 CD B:GLU51 2.9 5.3 1.0 OE1 B:GLU51 2.9 25.5 1.0 CD B:GLU127 2.9 2.0 1.0 CE1 B:HIS130 3.0 76.6 1.0 OE2 B:GLU127 3.5 66.9 1.0 FE B:FE301 3.6 30.7 1.0 CG B:HIS130 3.7 62.5 1.0 CG B:GLU127 4.1 53.7 1.0 CG B:GLU94 4.2 41.0 1.0 CG B:GLU51 4.2 24.8 1.0 NE2 B:HIS130 4.3 42.6 1.0 CB B:HIS130 4.3 44.6 1.0 CE2 B:TYR25 4.4 29.6 1.0 CA B:GLU127 4.4 26.5 1.0 OH B:TYR25 4.4 47.3 1.0 CB B:GLU127 4.5 19.9 1.0 CD2 B:HIS130 4.6 24.9 1.0 OE1 B:GLU18 4.7 43.5 1.0 CZ B:TYR25 4.8 53.3 1.0 OE2 B:GLU18 5.0 34.5 1.0

Iron binding site 6 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:27.4 occ:1.00 OE2 C:GLU127 1.9 36.0 1.0 OE1 C:GLU51 2.1 33.1 1.0 OE2 C:GLU18 2.2 34.6 1.0 ND1 C:HIS54 2.2 12.2 1.0 OE1 C:GLU18 2.3 48.7 1.0 CD C:GLU18 2.6 23.4 1.0 CD C:GLU127 2.8 15.6 1.0 CD C:GLU51 3.0 11.6 1.0 OE1 C:GLU127 3.1 28.1 1.0 CE1 C:HIS54 3.1 23.7 1.0 OE2 C:GLU51 3.2 44.5 1.0 CG C:HIS54 3.3 9.7 1.0 FE C:FE302 3.5 37.6 0.8 CB C:HIS54 3.6 18.1 1.0 CG C:GLU18 4.1 33.5 1.0 CG C:GLU127 4.2 26.3 1.0 CG2 C:ILE123 4.2 10.7 1.0 CA C:GLU51 4.2 16.9 1.0 NE2 C:HIS54 4.3 24.1 1.0 CG C:GLU51 4.3 29.3 1.0 CD2 C:HIS54 4.4 25.5 1.0 CB C:GLU51 4.6 12.7 1.0 CE1 C:HIS130 4.6 60.2 1.0 N C:GLU51 4.9 15.0 1.0 CB C:GLU18 5.0 23.6 1.0 ND1 C:HIS130 5.0 42.2 1.0 O C:ASP50 5.0 15.5 1.0

Iron binding site 7 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe302 b:37.6 occ:0.75 OE1 C:GLU127 2.0 28.1 1.0 OE2 C:GLU51 2.1 44.5 1.0 ND1 C:HIS130 2.2 42.2 1.0 OE1 C:GLU94 2.5 42.4 1.0 CE1 C:HIS130 2.7 60.2 1.0 CD C:GLU51 2.8 11.6 1.0 OE1 C:GLU51 2.9 33.1 1.0 CD C:GLU127 3.1 15.6 1.0 CD C:GLU94 3.1 35.3 1.0 OE2 C:GLU94 3.1 46.7 1.0 CG C:HIS130 3.4 47.9 1.0 OE2 C:GLU127 3.5 36.0 1.0 FE C:FE301 3.5 27.4 1.0 NE2 C:HIS130 4.0 44.3 1.0 CB C:HIS130 4.1 25.0 1.0 CG C:GLU51 4.1 29.3 1.0 CE2 C:TYR25 4.3 30.4 1.0 OH C:TYR25 4.3 47.1 1.0 CD2 C:HIS130 4.3 58.2 1.0 CG C:GLU127 4.3 26.3 1.0 CA C:GLU127 4.3 15.6 1.0 CG C:GLU94 4.4 33.7 1.0 CB C:GLU127 4.5 9.6 1.0 CZ C:TYR25 4.7 52.9 1.0 OE1 C:GLU18 4.7 48.7 1.0 ND1 C:HIS54 4.9 12.2 1.0

Iron binding site 8 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe200 b:22.4 occ:1.00 FE C:HEM200 0.0 22.4 1.0 ND C:HEM200 2.0 24.7 0.5 ND C:HEM200 2.0 25.4 0.5 NA C:HEM200 2.1 18.9 0.5 NA C:HEM200 2.1 23.9 0.5 NC C:HEM200 2.1 10.1 0.5 NC C:HEM200 2.1 27.0 0.5 NB C:HEM200 2.1 28.1 0.5 NB C:HEM200 2.1 22.7 0.5 SD C:MET52 2.3 12.8 1.0 SD D:MET52 2.5 13.7 1.0 C4D C:HEM200 3.0 19.0 0.5 C4D C:HEM200 3.0 30.7 0.5 C1D C:HEM200 3.0 24.4 0.5 C1A C:HEM200 3.0 17.3 0.5 C4C C:HEM200 3.0 2.0 0.5 C1A C:HEM200 3.1 28.5 0.5 C1D C:HEM200 3.1 12.6 0.5 C4C C:HEM200 3.1 14.7 0.5 C4A C:HEM200 3.1 17.6 0.5 C4A C:HEM200 3.1 22.5 0.5 C1C C:HEM200 3.1 16.2 0.5 C1B C:HEM200 3.1 17.4 0.5 C4B C:HEM200 3.1 25.9 0.5 C1B C:HEM200 3.1 23.2 0.5 C4B C:HEM200 3.1 25.7 0.5 C1C C:HEM200 3.1 22.4 0.5 CHA C:HEM200 3.4 12.6 0.5 CHA C:HEM200 3.4 19.0 0.5 CHD C:HEM200 3.4 30.7 0.5 CE C:MET52 3.4 10.4 1.0 CHD C:HEM200 3.4 9.2 0.5 CG C:MET52 3.5 12.2 1.0 CHB C:HEM200 3.5 27.9 0.5 CHB C:HEM200 3.5 21.9 0.5 CHC C:HEM200 3.5 20.8 0.5 CHC C:HEM200 3.5 26.9 0.5 CE D:MET52 3.6 8.7 1.0 CG D:MET52 3.6 11.4 1.0 CB C:MET52 4.2 14.9 1.0 C3D C:HEM200 4.2 23.8 0.5 C3D C:HEM200 4.3 24.3 0.5 C2A C:HEM200 4.3 4.5 0.5 C2D C:HEM200 4.3 21.4 0.5 C2D C:HEM200 4.3 19.9 0.5 C3C C:HEM200 4.3 18.3 0.5 C2A C:HEM200 4.3 7.5 0.5 C3A C:HEM200 4.3 25.6 0.5 C3A C:HEM200 4.3 27.7 0.5 C3C C:HEM200 4.3 28.4 0.5 C2C C:HEM200 4.3 11.5 0.5 C2B C:HEM200 4.3 16.3 0.5 C2C C:HEM200 4.3 19.2 0.5 C3B C:HEM200 4.3 26.7 0.5 CB D:MET52 4.3 15.7 1.0 C3B C:HEM200 4.3 33.7 0.5 C2B C:HEM200 4.3 24.3 0.5

Iron binding site 9 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe301 b:26.9 occ:1.00 ND1 D:HIS54 2.0 7.4 1.0 OE2 D:GLU127 2.1 32.4 1.0 OE1 D:GLU51 2.2 18.1 1.0 OE2 D:GLU18 2.2 25.2 1.0 OE1 D:GLU18 2.4 29.5 1.0 CD D:GLU18 2.7 19.4 1.0 CE1 D:HIS54 2.8 36.7 1.0 CD D:GLU127 2.8 22.4 1.0 OE1 D:GLU127 2.8 17.0 1.0 CD D:GLU51 2.9 9.8 1.0 OE2 D:GLU51 3.1 45.8 1.0 CG D:HIS54 3.1 14.3 1.0 CB D:HIS54 3.6 22.8 1.0 FE D:FE302 3.8 36.5 0.8 NE2 D:HIS54 3.9 21.2 1.0 CG2 D:ILE123 4.0 7.1 1.0 CD2 D:HIS54 4.1 28.5 1.0 CG D:GLU18 4.2 26.2 1.0 CG D:GLU127 4.3 34.9 1.0 CG D:GLU51 4.3 4.7 1.0 CA D:GLU51 4.3 16.7 1.0 CB D:GLU51 4.7 11.8 1.0 CE1 D:HIS130 4.8 77.2 1.0 O D:ASP50 4.9 16.2 1.0 N D:GLU51 5.0 5.0 1.0

Iron binding site 10 out of 20 in the E. Coli Bacterioferritin in Its As-Isolated Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of E. Coli Bacterioferritin in Its As-Isolated Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe302 b:36.5 occ:0.75 OE1 D:GLU94 2.3 45.6 1.0 OE1 D:GLU127 2.3 17.0 1.0 OE2 D:GLU51 2.3 45.8 1.0 ND1 D:HIS130 2.3 54.4 1.0 OE2 D:GLU94 2.6 25.3 1.0 CD D:GLU94 2.7 18.3 1.0 CD D:GLU51 3.0 9.8 1.0 CE1 D:HIS130 3.1 77.2 1.0 OE1 D:GLU51 3.2 18.1 1.0 CG D:HIS130 3.5 63.8 1.0 CD D:GLU127 3.5 22.4 1.0 FE D:FE301 3.8 26.9 1.0 CB D:HIS130 3.9 39.4 1.0 CG D:GLU51 4.1 4.7 1.0 OH D:TYR25 4.1 48.1 1.0 OE2 D:GLU127 4.2 32.4 1.0 CE2 D:TYR25 4.2 31.5 1.0 CG D:GLU94 4.2 54.4 1.0 NE2 D:HIS130 4.3 69.0 1.0 CA D:GLU127 4.3 21.7 1.0 CD2 D:HIS130 4.5 66.1 1.0 CG D:GLU127 4.6 34.9 1.0 CZ D:TYR25 4.6 53.5 1.0 CB D:GLU127 4.6 26.3 1.0 OE1 D:GLU18 4.8 29.5 1.0

A.Van Eerde, S.Wolterink-Van Loo, J.Van Der Oost, B.W.Dijkstra. Fortuitous Structure Determination of 'As-Isolated' Escherichia Coli Bacterioferritin in A Novel Crystal Form. Acta Crystallogr.,Sect.F V. 62 1061 2006.
ISSN: ISSN 1744-3091
PubMed: 17077480
DOI: 10.1107/S1744309106039583