Iron in PDB 4am4: Bacterioferritin From Blastochloris Viridis

The structure of Bacterioferritin From Blastochloris Viridis, PDB code: 4am4 was solved by W.Y.Wahlgren, H.Omran, D.Von Stetten, A.Royant, S.Van Der Post, G.Katona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	98.52 / 1.68
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	170.650, 170.650, 170.650, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.6

The binding sites of Iron atom in the Bacterioferritin From Blastochloris Viridis (pdb code 4am4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Bacterioferritin From Blastochloris Viridis, PDB code: 4am4:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in the Bacterioferritin From Blastochloris Viridis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bacterioferritin From Blastochloris Viridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1160 b:15.8 occ:1.00 FE A:HEM1160 0.0 15.8 1.0 NC A:HEM1160 2.0 15.1 1.0 NA A:HEM1160 2.0 17.7 1.0 ND A:HEM1160 2.0 18.1 1.0 NB A:HEM1160 2.0 15.1 1.0 SD B:MET52 2.3 16.0 1.0 SD A:MET52 2.3 15.6 1.0 C4D A:HEM1160 3.0 19.8 1.0 C4B A:HEM1160 3.0 17.0 1.0 C1A A:HEM1160 3.0 21.0 1.0 C1D A:HEM1160 3.0 17.8 1.0 C1B A:HEM1160 3.1 17.0 1.0 C1C A:HEM1160 3.1 16.1 1.0 C4C A:HEM1160 3.1 17.1 1.0 C4A A:HEM1160 3.1 18.6 1.0 CE B:MET52 3.4 16.1 1.0 CHA A:HEM1160 3.4 22.6 1.0 CE A:MET52 3.4 14.9 1.0 CHC A:HEM1160 3.4 15.6 1.0 CHB A:HEM1160 3.5 17.9 1.0 CHD A:HEM1160 3.5 17.8 1.0 CG B:MET52 3.6 13.5 1.0 CG A:MET52 3.6 14.8 1.0 CB B:MET52 4.2 14.4 1.0 CB A:MET52 4.2 14.3 1.0 C3B A:HEM1160 4.2 18.6 1.0 C3D A:HEM1160 4.3 23.5 1.0 C2A A:HEM1160 4.3 22.9 1.0 C2D A:HEM1160 4.3 19.6 1.0 C3C A:HEM1160 4.3 18.6 1.0 C3A A:HEM1160 4.3 20.0 1.0 C2C A:HEM1160 4.3 18.7 1.0 C2B A:HEM1160 4.3 18.6 1.0

Iron binding site 2 out of 5 in the Bacterioferritin From Blastochloris Viridis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bacterioferritin From Blastochloris Viridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1161 b:17.2 occ:1.00 OE2 A:GLU127 1.9 21.7 1.0 ND1 A:HIS54 2.0 21.6 1.0 OE1 A:GLU51 2.1 21.1 1.0 OE2 A:GLU18 2.2 26.1 1.0 OE1 A:GLU18 2.3 22.1 1.0 CD A:GLU18 2.6 21.4 1.0 CD A:GLU51 2.8 27.1 1.0 CD A:GLU127 2.9 22.8 1.0 OE2 A:GLU51 2.9 32.8 1.0 CE1 A:HIS54 3.0 21.6 1.0 OE1 A:GLU127 3.1 28.6 1.0 CG A:HIS54 3.1 17.5 1.0 O A:HOH2077 3.4 30.4 1.0 CB A:HIS54 3.6 15.7 1.0 FE A:FE1162 3.9 37.7 0.7 NE2 A:HIS54 4.1 22.1 1.0 CG A:GLU18 4.1 17.0 1.0 CG A:GLU51 4.2 18.8 1.0 CG A:GLU127 4.2 18.4 1.0 CD2 A:HIS54 4.2 20.9 1.0 O A:HOH2027 4.3 35.1 1.0 CA A:GLU51 4.3 17.0 1.0 CB A:GLU51 4.5 15.5 1.0 OH A:TYR101 4.6 23.8 1.0 CE2 A:TYR101 4.8 21.1 1.0

Iron binding site 3 out of 5 in the Bacterioferritin From Blastochloris Viridis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Bacterioferritin From Blastochloris Viridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1162 b:37.7 occ:0.70 OE2 A:GLU94 2.0 26.2 1.0 CD A:GLU94 2.7 31.2 1.0 OE1 A:GLU127 2.7 28.6 1.0 OE1 A:GLU94 2.8 28.0 1.0 OE2 A:GLU51 3.0 32.8 1.0 CD A:GLU51 3.2 27.1 1.0 OE1 A:GLU51 3.2 21.1 1.0 CD A:GLU127 3.2 22.8 1.0 O A:HOH2077 3.5 30.4 1.0 OE2 A:GLU47 3.5 15.2 0.3 OE2 A:GLU127 3.6 21.7 1.0 CB A:HIS130 3.9 18.9 1.0 FE A:FE1161 3.9 17.2 1.0 CD2 A:HIS130 3.9 22.3 1.0 OH A:TYR25 4.1 26.2 0.8 CG A:GLU94 4.1 27.7 1.0 CG A:HIS130 4.1 23.0 1.0 CE2 A:TYR25 4.1 19.3 0.8 CE2 A:TYR25 4.2 14.3 0.2 CG A:GLU51 4.2 18.8 1.0 CG A:GLU127 4.3 18.4 1.0 OH A:TYR25 4.3 13.3 0.2 CA A:GLU127 4.4 14.9 1.0 CD A:GLU47 4.6 14.6 0.3 CB A:GLU127 4.6 15.7 1.0 CZ A:TYR25 4.6 23.4 0.8 CZ A:TYR25 4.7 14.0 0.2 CG A:GLU47 4.8 14.1 0.3 O A:HOH2035 5.0 36.7 1.0

Iron binding site 4 out of 5 in the Bacterioferritin From Blastochloris Viridis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Bacterioferritin From Blastochloris Viridis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1160 b:16.9 occ:1.00 OE2 B:GLU127 2.0 21.1 1.0 ND1 B:HIS54 2.0 21.5 1.0 OE1 B:GLU51 2.1 21.2 1.0 OE2 B:GLU18 2.2 26.9 1.0 OE1 B:GLU18 2.3 20.3 1.0 CD B:GLU18 2.6 19.4 1.0 CD B:GLU51 2.8 26.9 1.0 CD B:GLU127 2.9 23.5 1.0 CE1 B:HIS54 3.0 24.1 1.0 OE2 B:GLU51 3.0 30.2 1.0 OE1 B:GLU127 3.1 28.4 1.0 CG B:HIS54 3.1 18.4 1.0 O B:HOH2067 3.3 32.7 1.0 CB B:HIS54 3.5 16.7 1.0 FE B:FE1161 3.9 38.0 0.7 NE2 B:HIS54 4.1 22.1 1.0 CG B:GLU18 4.1 16.1 1.0 CD2 B:HIS54 4.2 20.7 1.0 CG B:GLU51 4.2 19.4 1.0 CG B:GLU127 4.3 19.6 1.0 O B:HOH2022 4.3 36.0 1.0 CA B:GLU51 4.4 16.1 1.0 CB B:GLU51 4.6 15.1 1.0 OH B:TYR101 4.6 25.0 1.0 CE2 B:TYR101 4.8 21.0 1.0

Iron binding site 5 out of 5 in the Bacterioferritin From Blastochloris Viridis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Bacterioferritin From Blastochloris Viridis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1161 b:38.0 occ:0.70 OE2 B:GLU94 2.0 26.4 1.0 CD B:GLU94 2.7 30.2 1.0 OE1 B:GLU127 2.7 28.4 1.0 OE1 B:GLU94 2.8 28.0 1.0 OE2 B:GLU51 2.8 30.2 1.0 CD B:GLU51 3.1 26.9 1.0 OE1 B:GLU51 3.2 21.2 1.0 CD B:GLU127 3.3 23.5 1.0 OE2 B:GLU47 3.4 13.8 0.3 O B:HOH2067 3.6 32.7 1.0 OE2 B:GLU127 3.6 21.1 1.0 CB B:HIS130 3.9 19.5 1.0 CD2 B:HIS130 3.9 23.9 1.0 FE B:FE1160 3.9 16.9 1.0 CG B:HIS130 4.1 22.9 1.0 CE2 B:TYR25 4.1 18.3 0.8 OH B:TYR25 4.1 24.2 0.8 CG B:GLU94 4.1 28.4 1.0 CG B:GLU51 4.3 19.4 1.0 CE2 B:TYR25 4.3 12.4 0.2 OH B:TYR25 4.3 11.4 0.2 CG B:GLU127 4.4 19.6 1.0 CD B:GLU47 4.4 12.4 0.3 CA B:GLU127 4.4 16.4 1.0 CZ B:TYR25 4.6 21.8 0.8 CB B:GLU127 4.6 16.6 1.0 CZ B:TYR25 4.7 12.0 0.2 CG B:GLU47 4.7 13.1 0.3

W.Y.Wahlgren, H.Omran, D.Von Stetten, A.Royant, S.Van Der Post, G.Katona. Structural Characterization of Bacterioferritin From Blastochloris Viridis. Plos One V. 7 46992 2012.
ISSN: ESSN 1932-6203
PubMed: 23056552
DOI: 10.1371/JOURNAL.PONE.0046992