Iron in PDB 4am2: Bacterioferritin From Blastochloris Viridis

The structure of Bacterioferritin From Blastochloris Viridis, PDB code: 4am2 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)	98.26 / 1.80
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	170.200, 170.200, 170.200, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 19.2

The binding sites of Iron atom in the Bacterioferritin From Blastochloris Viridis (pdb code 4am2). 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: 4am2:
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:13.8 occ:1.00 FE A:HEM1160 0.0 13.8 1.0 NC A:HEM1160 1.9 13.4 1.0 NB A:HEM1160 2.0 12.8 1.0 NA A:HEM1160 2.0 15.8 1.0 ND A:HEM1160 2.1 16.1 1.0 SD B:MET52 2.3 13.3 1.0 SD A:MET52 2.3 12.8 1.0 C4C A:HEM1160 3.0 14.2 1.0 C1C A:HEM1160 3.0 13.1 1.0 C4B A:HEM1160 3.0 13.1 1.0 C1B A:HEM1160 3.1 15.2 1.0 C1D A:HEM1160 3.1 14.6 1.0 C4A A:HEM1160 3.1 16.2 1.0 C1A A:HEM1160 3.1 17.5 1.0 C4D A:HEM1160 3.1 16.3 1.0 CE A:MET52 3.4 11.6 1.0 CE B:MET52 3.4 12.3 1.0 CHB A:HEM1160 3.4 15.9 1.0 CHD A:HEM1160 3.4 15.4 1.0 CHC A:HEM1160 3.4 13.7 1.0 CG B:MET52 3.5 11.9 1.0 CHA A:HEM1160 3.5 18.0 1.0 CG A:MET52 3.5 11.8 1.0 CB A:MET52 4.1 11.8 1.0 CB B:MET52 4.2 12.2 1.0 C3C A:HEM1160 4.2 15.2 1.0 C2C A:HEM1160 4.3 15.9 1.0 C3B A:HEM1160 4.3 17.3 1.0 C2A A:HEM1160 4.3 22.3 1.0 C2D A:HEM1160 4.4 19.2 1.0 C3A A:HEM1160 4.4 20.2 1.0 C2B A:HEM1160 4.4 16.8 1.0 C3D A:HEM1160 4.4 20.5 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:17.5 occ:1.00 ND1 A:HIS54 2.0 19.6 1.0 OE1 A:GLU51 2.1 24.4 1.0 OE2 A:GLU127 2.1 21.5 1.0 OE2 A:GLU18 2.1 21.2 1.0 OE1 A:GLU18 2.5 20.6 1.0 CD A:GLU18 2.6 19.3 1.0 CD A:GLU51 2.9 28.0 1.0 CE1 A:HIS54 2.9 23.7 1.0 CG A:HIS54 3.1 18.4 1.0 CD A:GLU127 3.1 23.5 1.0 OE2 A:GLU51 3.2 41.6 1.0 O A:HOH2082 3.4 26.2 1.0 CB A:HIS54 3.5 14.1 1.0 OE1 A:GLU127 3.5 27.4 1.0 FE A:FE1162 4.0 23.6 0.4 NE2 A:HIS54 4.1 23.2 1.0 CG A:GLU18 4.1 15.6 1.0 CD2 A:HIS54 4.2 22.0 1.0 CG A:GLU51 4.2 18.3 1.0 O A:HOH2026 4.3 36.6 1.0 CA A:GLU51 4.4 13.4 1.0 CG A:GLU127 4.4 19.4 1.0 OH A:TYR101 4.5 24.9 1.0 CB A:GLU51 4.5 13.7 1.0 CE2 A:TYR101 4.7 20.3 1.0 CE1 A:HIS130 4.7 29.2 1.0 CD2 A:LEU123 4.9 22.6 1.0 ND1 A:HIS130 5.0 25.9 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:23.6 occ:0.40 ND1 A:HIS130 1.9 25.9 1.0 OE2 A:GLU94 1.9 25.1 1.0 OE1 A:GLU127 2.1 27.4 1.0 OE2 A:GLU51 2.5 41.6 1.0 CD A:GLU94 2.6 28.4 1.0 CE1 A:HIS130 2.7 29.2 1.0 OE1 A:GLU94 2.7 24.0 1.0 CG A:HIS130 3.0 23.1 1.0 CD A:GLU51 3.0 28.0 1.0 OE1 A:GLU51 3.2 24.4 1.0 CD A:GLU127 3.2 23.5 1.0 O A:HOH2082 3.4 26.2 1.0 CB A:HIS130 3.6 18.1 1.0 OE2 A:GLU127 3.6 21.5 1.0 NE2 A:HIS130 3.9 29.7 1.0 FE A:FE1161 4.0 17.5 1.0 OH A:TYR25 4.1 20.4 1.0 CD2 A:HIS130 4.1 25.0 1.0 CG A:GLU94 4.1 21.3 1.0 CE2 A:TYR25 4.1 17.3 1.0 CG A:GLU51 4.2 18.3 1.0 CA A:GLU127 4.4 14.0 1.0 CG A:GLU127 4.5 19.4 1.0 CZ A:TYR25 4.5 20.9 1.0 O A:HOH2121 4.6 36.3 1.0 CB A:GLU127 4.7 17.6 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:17.5 occ:1.00 ND1 B:HIS54 1.9 21.1 1.0 OE2 B:GLU127 2.0 19.1 1.0 OE2 B:GLU18 2.1 21.5 1.0 OE1 B:GLU51 2.2 28.4 1.0 OE1 B:GLU18 2.5 21.0 1.0 CD B:GLU18 2.6 18.7 1.0 CE1 B:HIS54 2.9 27.6 1.0 CD B:GLU51 2.9 27.0 1.0 CG B:HIS54 3.0 18.8 1.0 CD B:GLU127 3.0 20.8 1.0 OE2 B:GLU51 3.1 35.0 1.0 OE1 B:GLU127 3.4 26.9 1.0 CB B:HIS54 3.4 14.4 1.0 O B:HOH2075 3.5 25.4 1.0 FE B:FE1161 3.9 24.1 0.4 NE2 B:HIS54 4.0 24.2 1.0 CD2 B:HIS54 4.1 22.1 1.0 CG B:GLU18 4.1 14.2 1.0 O B:HOH2030 4.2 36.4 1.0 CG B:GLU51 4.3 18.0 1.0 CG B:GLU127 4.4 18.3 1.0 CA B:GLU51 4.4 15.6 1.0 OH B:TYR101 4.5 23.5 1.0 CB B:GLU51 4.5 15.7 1.0 CE2 B:TYR101 4.6 17.8 1.0 CE1 B:HIS130 4.7 28.7 1.0 CA B:HIS54 5.0 13.6 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:24.1 occ:0.40 OE2 B:GLU94 1.9 25.4 1.0 ND1 B:HIS130 1.9 27.4 1.0 OE1 B:GLU127 2.1 26.9 1.0 CD B:GLU94 2.6 27.4 1.0 CE1 B:HIS130 2.6 28.7 1.0 OE2 B:GLU51 2.7 35.0 1.0 OE1 B:GLU94 2.8 24.8 1.0 CD B:GLU51 3.0 27.0 1.0 OE1 B:GLU51 3.0 28.4 1.0 CG B:HIS130 3.1 22.1 1.0 CD B:GLU127 3.2 20.8 1.0 O B:HOH2075 3.4 25.4 1.0 CB B:HIS130 3.7 16.5 1.0 OE2 B:GLU127 3.7 19.1 1.0 NE2 B:HIS130 3.9 29.9 1.0 FE B:FE1160 3.9 17.5 1.0 OH B:TYR25 4.0 21.3 1.0 CG B:GLU94 4.1 20.8 1.0 CD2 B:HIS130 4.1 29.8 1.0 CG B:GLU51 4.1 18.0 1.0 CE2 B:TYR25 4.1 17.3 1.0 CG B:GLU127 4.4 18.3 1.0 CA B:GLU127 4.5 15.5 1.0 CZ B:TYR25 4.6 20.1 1.0 CB B:GLU127 4.7 17.3 1.0 O B:HOH2109 4.8 29.5 1.0

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