Iron in PDB 2fl0: Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin

The structure of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin, PDB code: 2fl0 was solved by L.Swartz, K.Kunchinskas, H.Li, T.L.Poulos, W.N.Lanzilotta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.57 / 2.70
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	124.480, 124.480, 285.112, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 25.6

The structure of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin also contains other interesting chemical elements:

Magnesium

(Mg)

13 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 22;

Binding sites:

The binding sites of Iron atom in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin (pdb code 2fl0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 22 binding sites of Iron where determined in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin, PDB code: 2fl0:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1601 b:36.9 occ:1.00 OE2 A:GLU127 1.8 69.4 1.0 OE1 A:GLU51 2.0 51.5 1.0 ND1 A:HIS54 2.0 31.0 1.0 OE1 A:GLU18 2.2 45.0 1.0 OE2 A:GLU18 2.7 41.2 1.0 CD A:GLU18 2.7 41.1 1.0 CE1 A:HIS54 2.8 33.7 1.0 CD A:GLU127 2.8 65.5 1.0 CD A:GLU51 2.9 47.4 1.0 OE2 A:GLU51 3.2 50.0 1.0 CG A:HIS54 3.2 33.7 1.0 OE1 A:GLU127 3.3 70.6 1.0 FE A:FE21602 3.5 55.0 1.0 CB A:HIS54 3.7 30.6 1.0 O A:HOH3023 3.9 38.5 1.0 CG2 A:ILE123 4.0 32.0 1.0 NE2 A:HIS54 4.0 31.9 1.0 CG A:GLU127 4.1 57.7 1.0 CD2 A:HIS54 4.2 32.4 1.0 CG A:GLU18 4.2 38.6 1.0 CG A:GLU51 4.3 46.5 1.0 CA A:GLU51 4.4 39.1 1.0 CB A:GLU51 4.7 39.4 1.0 CE1 A:HIS130 4.7 50.1 1.0 ND1 A:HIS130 4.8 49.5 1.0 CB A:GLU18 5.0 38.5 1.0

Iron binding site 2 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1602 b:55.0 occ:1.00 OE2 A:GLU51 1.8 50.0 1.0 OE1 A:GLU127 1.9 70.6 1.0 OE2 A:GLU94 2.0 49.6 1.0 ND1 A:HIS130 2.3 49.5 1.0 OE1 A:GLU94 2.5 51.9 1.0 CD A:GLU94 2.6 49.6 1.0 CD A:GLU127 2.9 65.5 1.0 CD A:GLU51 3.0 47.4 1.0 CE1 A:HIS130 3.1 50.1 1.0 OE2 A:GLU127 3.4 69.4 1.0 FE A:FE21601 3.5 36.9 1.0 CG A:HIS130 3.5 50.4 1.0 OE1 A:GLU51 3.5 51.5 1.0 O A:HOH3023 3.7 38.5 1.0 CB A:HIS130 3.9 45.8 1.0 CG A:GLU94 4.1 49.1 1.0 CG A:GLU127 4.2 57.7 1.0 CG A:GLU51 4.2 46.5 1.0 OH A:TYR25 4.3 41.4 1.0 NE2 A:HIS130 4.3 51.3 1.0 CB A:GLU127 4.4 45.2 1.0 CA A:GLU127 4.4 42.9 1.0 CE2 A:TYR25 4.5 37.1 1.0 CD2 A:HIS130 4.5 50.7 1.0 CE1 A:HIS54 4.6 33.7 1.0 ND1 A:HIS54 4.8 31.0 1.0 CZ A:TYR25 4.8 40.5 1.0 CB A:GLU94 5.0 43.8 1.0 OE1 A:GLU18 5.0 45.0 1.0

Iron binding site 3 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1603 b:41.0 occ:1.00 OD1 G:ASN148 2.6 34.3 1.0 OD1 A:ASN148 2.7 34.3 1.0 O G:HOH3007 2.8 26.0 1.0 OE1 A:GLN151 2.9 35.0 1.0 OD1 F:ASN148 2.9 37.2 1.0 OE1 F:GLN151 3.1 39.6 1.0 OE1 G:GLN151 3.1 35.8 1.0 CG G:ASN148 3.8 34.2 1.0 CG F:ASN148 3.8 36.3 1.0 CG A:ASN148 3.8 34.4 1.0 CD A:GLN151 3.9 29.6 1.0 CD F:GLN151 4.0 36.3 1.0 ND2 F:ASN148 4.1 36.0 1.0 CD G:GLN151 4.2 30.3 1.0 NE2 F:GLN151 4.3 36.3 1.0 NE2 A:GLN151 4.3 29.9 1.0 ND2 G:ASN148 4.4 37.4 1.0 ND2 A:ASN148 4.5 36.4 1.0 NE2 G:GLN151 4.6 27.9 1.0 O F:HOH1725 4.9 34.9 1.0 CB G:ASN148 4.9 29.8 1.0

Iron binding site 4 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe3001 b:56.2 occ:1.00 FE A:HEM3001 0.0 56.2 1.0 ND A:HEM3001 2.0 58.6 1.0 NA A:HEM3001 2.0 58.8 1.0 NC A:HEM3001 2.0 54.8 1.0 NB A:HEM3001 2.0 54.9 1.0 SD A:MET52 2.1 53.1 1.0 SD B:MET52 2.1 53.9 1.0 C1D A:HEM3001 3.1 58.2 1.0 C4D A:HEM3001 3.1 59.2 1.0 C1A A:HEM3001 3.1 59.9 1.0 C4A A:HEM3001 3.1 58.7 1.0 C4C A:HEM3001 3.1 55.4 1.0 C1C A:HEM3001 3.1 55.3 1.0 C4B A:HEM3001 3.1 54.4 1.0 C1B A:HEM3001 3.1 54.4 1.0 CHD A:HEM3001 3.4 56.1 1.0 CHA A:HEM3001 3.4 60.2 1.0 CE B:MET52 3.4 50.0 1.0 CE A:MET52 3.4 50.5 1.0 CHB A:HEM3001 3.4 56.0 1.0 CHC A:HEM3001 3.4 56.3 1.0 CG A:MET52 3.5 42.9 1.0 CG B:MET52 3.6 41.9 1.0 C3D A:HEM3001 4.3 59.6 1.0 C2A A:HEM3001 4.3 60.0 1.0 C2D A:HEM3001 4.3 59.4 1.0 C3A A:HEM3001 4.3 59.5 1.0 C2C A:HEM3001 4.3 53.7 1.0 CB A:MET52 4.3 33.6 1.0 C3C A:HEM3001 4.4 55.8 1.0 C2B A:HEM3001 4.4 54.4 1.0 C3B A:HEM3001 4.4 53.3 1.0 CB B:MET52 4.4 33.8 1.0

Iron binding site 5 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1605 b:55.4 occ:1.00 OE1 B:GLU51 1.8 55.9 1.0 OE2 B:GLU94 1.9 48.3 1.0 OE1 B:GLU127 2.0 71.1 1.0 ND1 B:HIS130 2.1 50.3 1.0 CD B:GLU94 2.6 46.7 1.0 OE1 B:GLU94 2.7 48.5 1.0 CE1 B:HIS130 2.8 50.1 1.0 CD B:GLU51 2.9 50.0 1.0 CD B:GLU127 3.0 65.6 1.0 CG B:HIS130 3.3 49.2 1.0 OE2 B:GLU51 3.3 53.0 1.0 OE2 B:GLU127 3.4 69.0 1.0 FE B:FE21606 3.6 39.0 1.0 CB B:HIS130 3.8 44.8 1.0 O B:HOH1731 3.9 36.4 1.0 CG B:GLU94 4.0 46.8 1.0 NE2 B:HIS130 4.0 51.2 1.0 CG B:GLU51 4.1 46.6 1.0 CD2 B:HIS130 4.3 49.6 1.0 CG B:GLU127 4.3 57.6 1.0 CA B:GLU127 4.4 44.4 1.0 CE2 B:TYR25 4.5 36.2 1.0 OH B:TYR25 4.5 39.1 1.0 CB B:GLU127 4.6 46.0 1.0 CE1 B:HIS54 4.7 28.5 1.0 ND1 B:HIS54 4.8 24.6 1.0

Iron binding site 6 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1606 b:39.0 occ:1.00 OE2 B:GLU127 1.9 69.0 1.0 OE2 B:GLU51 2.0 53.0 1.0 ND1 B:HIS54 2.2 24.6 1.0 OE1 B:GLU18 2.2 49.6 1.0 OE2 B:GLU18 2.7 42.9 1.0 CD B:GLU18 2.8 43.6 1.0 CD B:GLU127 3.0 65.6 1.0 CE1 B:HIS54 3.0 28.5 1.0 CD B:GLU51 3.0 50.0 1.0 CG B:HIS54 3.3 31.2 1.0 OE1 B:GLU127 3.4 71.1 1.0 OE1 B:GLU51 3.5 55.9 1.0 FE B:FE21605 3.6 55.4 1.0 CB B:HIS54 3.7 28.5 1.0 O B:HOH1731 3.8 36.4 1.0 CG2 B:ILE123 3.9 35.1 1.0 NE2 B:HIS54 4.2 29.9 1.0 CG B:GLU127 4.2 57.6 1.0 CG B:GLU18 4.3 40.6 1.0 CD2 B:HIS54 4.3 31.8 1.0 CG B:GLU51 4.4 46.6 1.0 CA B:GLU51 4.4 38.8 1.0 CB B:GLU51 4.6 39.5 1.0 CE1 B:HIS130 4.7 50.1 1.0 OE2 B:GLU94 4.7 48.3 1.0 ND1 B:HIS130 4.9 50.3 1.0 CB B:GLU18 4.9 39.4 1.0

Iron binding site 7 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1607 b:43.3 occ:1.00 O D:HOH1742 2.7 37.4 1.0 OD1 D:ASN148 2.8 36.9 1.0 OE1 B:GLN151 2.8 32.6 1.0 OE1 D:GLN151 3.1 28.3 1.0 OD1 B:ASN148 3.1 36.2 1.0 CD B:GLN151 3.8 26.9 1.0 CG D:ASN148 3.9 36.9 1.0 CD D:GLN151 4.1 28.7 1.0 NE2 B:GLN151 4.1 23.2 1.0 CG B:ASN148 4.1 32.5 1.0 NE2 D:GLN151 4.4 26.3 1.0 ND2 B:ASN148 4.5 33.6 1.0 ND2 D:ASN148 4.5 40.3 1.0 CB D:ASN148 5.0 33.5 1.0

Iron binding site 8 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1608 b:41.0 occ:1.00 OE2 C:GLU127 1.9 48.6 1.0 OE1 C:GLU51 2.0 51.7 1.0 OE1 C:GLU18 2.2 41.6 1.0 ND1 C:HIS54 2.3 33.9 1.0 OE2 C:GLU18 2.7 41.6 1.0 CD C:GLU18 2.8 38.1 1.0 CD C:GLU127 2.9 44.3 1.0 CD C:GLU51 3.1 47.2 1.0 CE1 C:HIS54 3.1 33.9 1.0 OE1 C:GLU127 3.2 48.9 1.0 O C:HOH3003 3.3 33.5 1.0 CG C:HIS54 3.4 35.0 1.0 OE2 C:GLU51 3.4 52.4 1.0 FE C:FE21610 3.5 54.0 1.0 CB C:HIS54 3.8 30.8 1.0 CG2 C:ILE123 4.1 31.0 1.0 CG C:GLU127 4.3 39.9 1.0 CG C:GLU18 4.3 34.4 1.0 NE2 C:HIS54 4.3 32.2 1.0 CA C:GLU51 4.4 30.1 1.0 CG C:GLU51 4.4 42.5 1.0 CD2 C:HIS54 4.5 34.2 1.0 CB C:GLU51 4.6 37.6 1.0 CB C:GLU18 5.0 29.8 1.0

Iron binding site 9 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1610 b:54.0 occ:1.00 OE1 C:GLU127 1.9 48.9 1.0 OE2 C:GLU51 2.0 52.4 1.0 OE1 C:GLU94 2.2 50.8 1.0 ND1 C:HIS130 2.6 47.7 1.0 OE2 C:GLU94 2.7 49.8 1.0 CD C:GLU94 2.8 48.3 1.0 CD C:GLU51 3.0 47.2 1.0 CD C:GLU127 3.0 44.3 1.0 O C:HOH3003 3.2 33.5 1.0 CE1 C:HIS130 3.3 48.7 1.0 OE1 C:GLU51 3.4 51.7 1.0 FE C:FE21608 3.5 41.0 1.0 OE2 C:GLU127 3.5 48.6 1.0 CG C:HIS130 3.7 47.0 1.0 CB C:HIS130 4.2 41.1 1.0 CG C:GLU94 4.3 44.6 1.0 CE2 C:TYR25 4.3 32.7 1.0 CA C:GLU127 4.3 33.3 1.0 CG C:GLU51 4.3 42.5 1.0 CG C:GLU127 4.3 39.9 1.0 OH C:TYR25 4.4 35.1 1.0 NE2 C:HIS130 4.5 50.0 1.0 CB C:GLU127 4.5 31.4 1.0 CD2 C:HIS130 4.7 49.9 1.0 CE1 C:HIS54 4.8 33.9 1.0 ND1 C:HIS54 4.9 33.9 1.0 CZ C:TYR25 4.9 34.6 1.0

Iron binding site 10 out of 22 in the Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Oxidized (All Ferric) Form of the Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe3002 b:32.9 occ:1.00 FE C:HEM3002 0.0 32.9 1.0 ND C:HEM3002 2.0 33.3 1.0 NA C:HEM3002 2.0 31.8 1.0 NC C:HEM3002 2.0 32.1 1.0 NB C:HEM3002 2.0 30.8 1.0 SD D:MET52 2.1 28.8 1.0 SD C:MET52 2.1 31.1 1.0 C1D C:HEM3002 3.0 33.2 1.0 C1C C:HEM3002 3.1 31.4 1.0 C4D C:HEM3002 3.1 34.5 1.0 C4C C:HEM3002 3.1 34.2 1.0 C4A C:HEM3002 3.1 30.2 1.0 C1A C:HEM3002 3.1 33.6 1.0 C4B C:HEM3002 3.1 29.9 1.0 C1B C:HEM3002 3.1 30.3 1.0 CE C:MET52 3.4 28.4 1.0 CHD C:HEM3002 3.4 33.6 1.0 CHC C:HEM3002 3.4 30.9 1.0 CHA C:HEM3002 3.4 31.8 1.0 CHB C:HEM3002 3.4 31.8 1.0 CE D:MET52 3.4 28.1 1.0 CG D:MET52 3.5 25.6 1.0 CG C:MET52 3.5 26.6 1.0 CB D:MET52 4.2 23.7 1.0 C2D C:HEM3002 4.3 33.6 1.0 C3D C:HEM3002 4.3 35.1 1.0 C3A C:HEM3002 4.3 31.4 1.0 C2A C:HEM3002 4.3 32.0 1.0 C2C C:HEM3002 4.3 34.4 1.0 C3C C:HEM3002 4.3 34.3 1.0 C3B C:HEM3002 4.3 31.8 1.0 C2B C:HEM3002 4.3 33.1 1.0 CB C:MET52 4.4 25.1 1.0

L.Swartz, M.Kuchinskas, H.Li, T.L.Poulos, W.N.Lanzilotta. Redox-Dependent Structural Changes in the Azotobacter Vinelandii Bacterioferritin: New Insights Into the Ferroxidase and Iron Transport Mechanism(,). Biochemistry V. 45 4421 2006.
ISSN: ISSN 0006-2960
PubMed: 16584178
DOI: 10.1021/BI060146W