Iron in PDB 3bkn: The Structure of Mycobacterial Bacterioferritin

The structure of The Structure of Mycobacterial Bacterioferritin, PDB code: 3bkn was solved by R.Janowski, T.Auerbach-Nevo, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.64 / 2.72
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	181.523, 151.520, 116.715, 90.00, 128.08, 90.00
R / Rfree (%)	17.9 / 22.8

The structure of The Structure of Mycobacterial Bacterioferritin also contains other interesting chemical elements:

Magnesium	(Mg)	12 atoms
Zinc	(Zn)	24 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Iron atom in the The Structure of Mycobacterial Bacterioferritin (pdb code 3bkn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the The Structure of Mycobacterial Bacterioferritin, PDB code: 3bkn:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:42.3 occ:0.50 FE B:HEM301 0.0 42.3 0.5 FE B:HEM301 0.2 48.6 0.5 NC B:HEM301 1.9 48.7 0.5 ND B:HEM301 2.0 49.9 0.5 ND B:HEM301 2.1 42.9 0.5 NA B:HEM301 2.1 43.7 0.5 NB B:HEM301 2.1 42.3 0.5 NC B:HEM301 2.1 43.4 0.5 NB B:HEM301 2.2 49.8 0.5 NA B:HEM301 2.2 49.7 0.5 SD A:MET52 2.4 43.2 1.0 SD B:MET52 2.5 42.1 1.0 C4C B:HEM301 2.9 48.7 0.5 C1D B:HEM301 3.0 49.8 0.5 C1C B:HEM301 3.0 48.7 0.5 C4D B:HEM301 3.1 43.2 0.5 C4B B:HEM301 3.1 42.2 0.5 C1C B:HEM301 3.1 42.6 0.5 C1D B:HEM301 3.1 43.1 0.5 C4D B:HEM301 3.1 50.0 0.5 C1A B:HEM301 3.1 43.9 0.5 C4A B:HEM301 3.1 43.7 0.5 C1B B:HEM301 3.1 42.8 0.5 C4C B:HEM301 3.1 43.9 0.5 C4B B:HEM301 3.1 49.3 0.5 C1A B:HEM301 3.2 49.8 0.5 C1B B:HEM301 3.2 50.1 0.5 C4A B:HEM301 3.2 49.5 0.5 CHD B:HEM301 3.3 49.9 0.5 CHC B:HEM301 3.4 48.8 0.5 CHC B:HEM301 3.4 42.6 0.5 CHA B:HEM301 3.4 43.5 0.5 CE A:MET52 3.4 43.2 1.0 CG B:MET52 3.4 42.3 1.0 CHB B:HEM301 3.5 43.7 0.5 CHD B:HEM301 3.5 43.8 0.5 CHA B:HEM301 3.5 49.8 0.5 CG A:MET52 3.5 43.8 1.0 CHB B:HEM301 3.6 49.8 0.5 CE B:MET52 3.6 42.7 1.0 C3C B:HEM301 4.2 48.2 0.5 C2D B:HEM301 4.3 49.7 0.5 C2C B:HEM301 4.3 49.0 0.5 C3D B:HEM301 4.3 49.9 0.5 C3D B:HEM301 4.3 43.2 0.5 C3B B:HEM301 4.3 42.2 0.5 CB B:MET52 4.3 43.1 1.0 C2D B:HEM301 4.4 43.0 0.5 C3B B:HEM301 4.4 49.5 0.5 C3A B:HEM301 4.4 43.4 0.5 C2A B:HEM301 4.4 44.0 0.5 CB A:MET52 4.4 44.4 1.0 C2C B:HEM301 4.4 43.0 0.5 C3C B:HEM301 4.4 43.1 0.5 C2B B:HEM301 4.4 42.1 0.5 C2B B:HEM301 4.5 49.6 0.5 C3A B:HEM301 4.5 49.4 0.5 C2A B:HEM301 4.5 49.6 0.5

Iron binding site 2 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:48.6 occ:0.50 FE B:HEM301 0.0 48.6 0.5 FE B:HEM301 0.2 42.3 0.5 ND B:HEM301 1.9 42.9 0.5 NC B:HEM301 2.0 43.4 0.5 ND B:HEM301 2.1 49.9 0.5 NA B:HEM301 2.1 49.7 0.5 NC B:HEM301 2.1 48.7 0.5 NB B:HEM301 2.1 49.8 0.5 NA B:HEM301 2.1 43.7 0.5 NB B:HEM301 2.2 42.3 0.5 SD B:MET52 2.4 42.1 1.0 SD A:MET52 2.4 43.2 1.0 C1D B:HEM301 2.9 43.1 0.5 C4D B:HEM301 3.0 43.2 0.5 C4C B:HEM301 3.0 43.9 0.5 C4A B:HEM301 3.1 49.5 0.5 C1C B:HEM301 3.1 42.6 0.5 C1D B:HEM301 3.1 49.8 0.5 C1C B:HEM301 3.1 48.7 0.5 C4C B:HEM301 3.1 48.7 0.5 C4D B:HEM301 3.1 50.0 0.5 C1B B:HEM301 3.1 50.1 0.5 C1A B:HEM301 3.1 43.9 0.5 C1A B:HEM301 3.1 49.8 0.5 C4B B:HEM301 3.1 49.3 0.5 C4B B:HEM301 3.2 42.2 0.5 C4A B:HEM301 3.2 43.7 0.5 C1B B:HEM301 3.3 42.8 0.5 CHD B:HEM301 3.3 43.8 0.5 CHA B:HEM301 3.4 43.5 0.5 CHB B:HEM301 3.4 49.8 0.5 CHC B:HEM301 3.4 48.8 0.5 CHC B:HEM301 3.4 42.6 0.5 CHA B:HEM301 3.4 49.8 0.5 CG B:MET52 3.5 42.3 1.0 CHD B:HEM301 3.5 49.9 0.5 CE B:MET52 3.5 42.7 1.0 CG A:MET52 3.5 43.8 1.0 CE A:MET52 3.5 43.2 1.0 CHB B:HEM301 3.6 43.7 0.5 C3D B:HEM301 4.2 43.2 0.5 C2D B:HEM301 4.2 43.0 0.5 C3B B:HEM301 4.3 49.5 0.5 C3C B:HEM301 4.3 43.1 0.5 C3D B:HEM301 4.3 49.9 0.5 CB A:MET52 4.3 44.4 1.0 CB B:MET52 4.3 43.1 1.0 C2D B:HEM301 4.4 49.7 0.5 C2C B:HEM301 4.4 43.0 0.5 C3C B:HEM301 4.4 48.2 0.5 C3A B:HEM301 4.4 49.4 0.5 C2C B:HEM301 4.4 49.0 0.5 C2A B:HEM301 4.4 49.6 0.5 C3B B:HEM301 4.4 42.2 0.5 C2B B:HEM301 4.4 49.6 0.5 C2A B:HEM301 4.4 44.0 0.5 C3A B:HEM301 4.5 43.4 0.5 C2B B:HEM301 4.6 42.1 0.5

Iron binding site 3 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:44.9 occ:0.50 FE C:HEM301 0.0 44.9 0.5 FE C:HEM301 0.1 42.0 0.5 NB C:HEM301 2.0 40.7 0.5 NC C:HEM301 2.0 41.6 0.5 NA C:HEM301 2.1 44.7 0.5 ND C:HEM301 2.1 45.1 0.5 NC C:HEM301 2.1 43.9 0.5 NB C:HEM301 2.1 44.4 0.5 NA C:HEM301 2.1 42.2 0.5 ND C:HEM301 2.2 41.6 0.5 SD C:MET52 2.4 41.9 1.0 SD D:MET52 2.6 45.1 1.0 C4B C:HEM301 2.9 40.7 0.5 C1B C:HEM301 3.0 40.9 0.5 C1C C:HEM301 3.0 41.6 0.5 C4C C:HEM301 3.1 44.0 0.5 C1A C:HEM301 3.1 45.3 0.5 C4A C:HEM301 3.1 44.9 0.5 C1D C:HEM301 3.1 45.4 0.5 C1C C:HEM301 3.1 43.7 0.5 C4A C:HEM301 3.1 42.8 0.5 C4C C:HEM301 3.1 41.3 0.5 C4B C:HEM301 3.1 44.2 0.5 C4D C:HEM301 3.1 45.2 0.5 C1B C:HEM301 3.1 44.3 0.5 C1A C:HEM301 3.1 42.4 0.5 C1D C:HEM301 3.2 41.9 0.5 C4D C:HEM301 3.2 42.4 0.5 CHC C:HEM301 3.3 41.2 0.5 CHB C:HEM301 3.4 42.0 0.5 CHD C:HEM301 3.4 45.0 0.5 CE D:MET52 3.4 43.7 1.0 CHC C:HEM301 3.4 43.9 0.5 CHA C:HEM301 3.4 45.4 0.5 CHB C:HEM301 3.5 45.3 0.5 CG C:MET52 3.5 42.9 1.0 CHD C:HEM301 3.5 42.5 0.5 CHA C:HEM301 3.5 42.6 0.5 CG D:MET52 3.6 44.1 1.0 CE C:MET52 3.6 41.9 1.0 C3B C:HEM301 4.1 41.5 0.5 CB C:MET52 4.2 43.2 1.0 C2B C:HEM301 4.3 41.4 0.5 C3B C:HEM301 4.3 44.3 0.5 C3D C:HEM301 4.3 45.9 0.5 C3C C:HEM301 4.3 40.9 0.5 C3C C:HEM301 4.3 44.1 0.5 C2A C:HEM301 4.4 46.1 0.5 C2D C:HEM301 4.4 45.6 0.5 C3A C:HEM301 4.4 45.6 0.5 C2C C:HEM301 4.4 41.9 0.5 C2C C:HEM301 4.4 44.6 0.5 C3A C:HEM301 4.4 42.7 0.5 C2B C:HEM301 4.4 43.8 0.5 C3D C:HEM301 4.4 43.0 0.5 C2A C:HEM301 4.4 43.4 0.5 C2D C:HEM301 4.5 42.6 0.5 CB D:MET52 4.5 44.0 1.0

Iron binding site 4 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:42.0 occ:0.50 FE C:HEM301 0.0 42.0 0.5 FE C:HEM301 0.1 44.9 0.5 NA C:HEM301 1.9 44.7 0.5 ND C:HEM301 2.0 45.1 0.5 NA C:HEM301 2.1 42.2 0.5 ND C:HEM301 2.1 41.6 0.5 NB C:HEM301 2.1 40.7 0.5 NC C:HEM301 2.1 41.6 0.5 NB C:HEM301 2.1 44.4 0.5 NC C:HEM301 2.2 43.9 0.5 SD C:MET52 2.4 41.9 1.0 SD D:MET52 2.6 45.1 1.0 C1A C:HEM301 2.9 45.3 0.5 C4A C:HEM301 3.0 44.9 0.5 C4D C:HEM301 3.0 45.2 0.5 C4B C:HEM301 3.1 40.7 0.5 C1A C:HEM301 3.1 42.4 0.5 C4C C:HEM301 3.1 41.3 0.5 C4A C:HEM301 3.1 42.8 0.5 C4D C:HEM301 3.1 42.4 0.5 C1B C:HEM301 3.1 40.9 0.5 C1D C:HEM301 3.1 41.9 0.5 C1D C:HEM301 3.1 45.4 0.5 C1B C:HEM301 3.1 44.3 0.5 C1C C:HEM301 3.1 41.6 0.5 C4B C:HEM301 3.2 44.2 0.5 C4C C:HEM301 3.2 44.0 0.5 C1C C:HEM301 3.2 43.7 0.5 CHA C:HEM301 3.3 45.4 0.5 CHB C:HEM301 3.4 45.3 0.5 CHA C:HEM301 3.4 42.6 0.5 CE D:MET52 3.4 43.7 1.0 CHC C:HEM301 3.4 41.2 0.5 CHB C:HEM301 3.4 42.0 0.5 CHD C:HEM301 3.4 42.5 0.5 CHD C:HEM301 3.5 45.0 0.5 CHC C:HEM301 3.5 43.9 0.5 CG C:MET52 3.5 42.9 1.0 CG D:MET52 3.6 44.1 1.0 CE C:MET52 3.6 41.9 1.0 C2A C:HEM301 4.2 46.1 0.5 C3B C:HEM301 4.2 41.5 0.5 C3A C:HEM301 4.2 45.6 0.5 C3D C:HEM301 4.3 45.9 0.5 CB C:MET52 4.3 43.2 1.0 C3D C:HEM301 4.3 43.0 0.5 C3C C:HEM301 4.3 40.9 0.5 C3B C:HEM301 4.3 44.3 0.5 C2D C:HEM301 4.3 45.6 0.5 C2D C:HEM301 4.4 42.6 0.5 C2A C:HEM301 4.4 43.4 0.5 C3A C:HEM301 4.4 42.7 0.5 C2B C:HEM301 4.4 41.4 0.5 CB D:MET52 4.4 44.0 1.0 C2B C:HEM301 4.4 43.8 0.5 C2C C:HEM301 4.4 41.9 0.5 C3C C:HEM301 4.5 44.1 0.5 C2C C:HEM301 4.5 44.6 0.5

Iron binding site 5 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:49.3 occ:0.50 FE E:HEM301 0.0 49.3 0.5 FE E:HEM301 0.1 47.6 0.5 NB E:HEM301 2.1 47.7 0.5 ND E:HEM301 2.1 49.4 0.5 NA E:HEM301 2.1 49.3 0.5 NA E:HEM301 2.1 48.0 0.5 NC E:HEM301 2.1 47.8 0.5 NB E:HEM301 2.1 49.2 0.5 NC E:HEM301 2.1 49.3 0.5 ND E:HEM301 2.1 47.6 0.5 SD E:MET52 2.4 44.1 1.0 SD F:MET52 2.4 44.4 1.0 C1D E:HEM301 3.1 49.6 0.5 C4B E:HEM301 3.1 47.5 0.5 C4A E:HEM301 3.1 49.9 0.5 C4A E:HEM301 3.1 48.1 0.5 C4C E:HEM301 3.1 47.5 0.5 C1B E:HEM301 3.1 48.3 0.5 C1D E:HEM301 3.1 48.3 0.5 C4C E:HEM301 3.1 49.8 0.5 C1B E:HEM301 3.1 49.2 0.5 C1A E:HEM301 3.1 50.1 0.5 C4B E:HEM301 3.1 49.2 0.5 C4D E:HEM301 3.1 50.4 0.5 C1C E:HEM301 3.1 47.9 0.5 C1A E:HEM301 3.1 48.7 0.5 C1C E:HEM301 3.1 49.2 0.5 C4D E:HEM301 3.1 48.1 0.5 CG E:MET52 3.4 44.0 1.0 CHD E:HEM301 3.4 50.0 0.5 CHB E:HEM301 3.4 50.0 0.5 CHD E:HEM301 3.4 48.4 0.5 CHB E:HEM301 3.4 48.4 0.5 CHC E:HEM301 3.4 47.8 0.5 CHC E:HEM301 3.4 49.3 0.5 CHA E:HEM301 3.5 50.2 0.5 CHA E:HEM301 3.5 48.4 0.5 CE F:MET52 3.5 44.1 1.0 CG F:MET52 3.5 43.8 1.0 CE E:MET52 3.6 44.8 1.0 C3B E:HEM301 4.2 47.7 0.5 C3B E:HEM301 4.3 48.9 0.5 CB E:MET52 4.3 44.4 1.0 C3D E:HEM301 4.3 50.5 0.5 C3D E:HEM301 4.3 48.6 0.5 C2D E:HEM301 4.3 50.0 0.5 C3C E:HEM301 4.3 47.3 0.5 CB F:MET52 4.4 44.5 1.0 C2D E:HEM301 4.4 48.3 0.5 C3C E:HEM301 4.4 49.5 0.5 C2B E:HEM301 4.4 47.9 0.5 C3A E:HEM301 4.4 48.3 0.5 C2A E:HEM301 4.4 50.6 0.5 C3A E:HEM301 4.4 50.0 0.5 C2B E:HEM301 4.4 49.0 0.5 C2A E:HEM301 4.4 48.9 0.5 C2C E:HEM301 4.4 47.7 0.5 C2C E:HEM301 4.4 49.7 0.5

Iron binding site 6 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe301 b:47.6 occ:0.50 FE E:HEM301 0.0 47.6 0.5 FE E:HEM301 0.1 49.3 0.5 NA E:HEM301 2.0 49.3 0.5 ND E:HEM301 2.1 49.4 0.5 NA E:HEM301 2.1 48.0 0.5 ND E:HEM301 2.1 47.6 0.5 NB E:HEM301 2.1 47.7 0.5 NC E:HEM301 2.1 47.8 0.5 NB E:HEM301 2.1 49.2 0.5 NC E:HEM301 2.1 49.3 0.5 SD E:MET52 2.3 44.1 1.0 SD F:MET52 2.5 44.4 1.0 C4A E:HEM301 3.0 49.9 0.5 C1D E:HEM301 3.1 48.3 0.5 C1D E:HEM301 3.1 49.6 0.5 C1A E:HEM301 3.1 50.1 0.5 C4A E:HEM301 3.1 48.1 0.5 C4C E:HEM301 3.1 47.5 0.5 C4D E:HEM301 3.1 50.4 0.5 C1A E:HEM301 3.1 48.7 0.5 C1B E:HEM301 3.1 49.2 0.5 C4B E:HEM301 3.1 47.5 0.5 C1B E:HEM301 3.1 48.3 0.5 C4C E:HEM301 3.1 49.8 0.5 C4D E:HEM301 3.1 48.1 0.5 C4B E:HEM301 3.1 49.2 0.5 C1C E:HEM301 3.1 47.9 0.5 C1C E:HEM301 3.1 49.2 0.5 CG E:MET52 3.3 44.0 1.0 CHB E:HEM301 3.4 50.0 0.5 CHD E:HEM301 3.4 48.4 0.5 CHD E:HEM301 3.4 50.0 0.5 CHB E:HEM301 3.4 48.4 0.5 CHA E:HEM301 3.4 50.2 0.5 CHC E:HEM301 3.4 47.8 0.5 CHA E:HEM301 3.5 48.4 0.5 CHC E:HEM301 3.5 49.3 0.5 CE E:MET52 3.5 44.8 1.0 CE F:MET52 3.5 44.1 1.0 CG F:MET52 3.6 43.8 1.0 CB E:MET52 4.2 44.4 1.0 C3B E:HEM301 4.3 47.7 0.5 C3B E:HEM301 4.3 48.9 0.5 C3D E:HEM301 4.3 50.5 0.5 C3D E:HEM301 4.3 48.6 0.5 C2D E:HEM301 4.3 50.0 0.5 C2D E:HEM301 4.3 48.3 0.5 C2A E:HEM301 4.3 50.6 0.5 C3A E:HEM301 4.3 50.0 0.5 C3C E:HEM301 4.4 47.3 0.5 C3A E:HEM301 4.4 48.3 0.5 C2A E:HEM301 4.4 48.9 0.5 C3C E:HEM301 4.4 49.5 0.5 C2B E:HEM301 4.4 49.0 0.5 C2B E:HEM301 4.4 47.9 0.5 CB F:MET52 4.4 44.5 1.0 C2C E:HEM301 4.4 47.7 0.5 C2C E:HEM301 4.4 49.7 0.5

Iron binding site 7 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe301 b:31.8 occ:0.50 FE H:HEM301 0.0 31.8 0.5 FE H:HEM301 0.1 51.0 0.5 ND H:HEM301 2.0 51.2 0.5 ND H:HEM301 2.1 31.7 0.5 NC H:HEM301 2.1 50.8 0.5 NA H:HEM301 2.1 32.2 0.5 NC H:HEM301 2.1 31.0 0.5 NB H:HEM301 2.1 31.3 0.5 NA H:HEM301 2.1 51.1 0.5 NB H:HEM301 2.2 50.5 0.5 SD H:MET52 2.5 44.4 1.0 SD G:MET52 2.5 43.3 1.0 C1D H:HEM301 3.0 51.5 0.5 C4D H:HEM301 3.0 52.2 0.5 C4C H:HEM301 3.0 51.0 0.5 C1A H:HEM301 3.1 52.3 0.5 C4D H:HEM301 3.1 33.5 0.5 C4A H:HEM301 3.1 32.5 0.5 C1C H:HEM301 3.1 50.3 0.5 C1D H:HEM301 3.1 31.7 0.5 C4B H:HEM301 3.1 30.9 0.5 C4C H:HEM301 3.1 31.4 0.5 C1B H:HEM301 3.1 31.9 0.5 C1C H:HEM301 3.1 31.0 0.5 C1A H:HEM301 3.1 33.5 0.5 C4A H:HEM301 3.1 51.0 0.5 C4B H:HEM301 3.2 50.6 0.5 C1B H:HEM301 3.2 50.8 0.5 CHA H:HEM301 3.4 52.1 0.5 CHD H:HEM301 3.4 51.7 0.5 CHC H:HEM301 3.4 31.1 0.5 CHA H:HEM301 3.4 33.2 0.5 CHB H:HEM301 3.4 32.4 0.5 CE H:MET52 3.4 44.2 1.0 CG H:MET52 3.4 43.2 1.0 CHC H:HEM301 3.4 50.5 0.5 CHD H:HEM301 3.4 32.7 0.5 CE G:MET52 3.5 44.4 1.0 CHB H:HEM301 3.5 51.4 0.5 CG G:MET52 3.6 43.2 1.0 C3D H:HEM301 4.2 52.5 0.5 C2D H:HEM301 4.3 51.8 0.5 C3B H:HEM301 4.3 31.6 0.5 C3D H:HEM301 4.3 33.6 0.5 C3C H:HEM301 4.3 50.8 0.5 C2D H:HEM301 4.3 32.9 0.5 C3C H:HEM301 4.4 31.7 0.5 C3B H:HEM301 4.4 51.1 0.5 CB H:MET52 4.4 43.5 1.0 C2A H:HEM301 4.4 52.2 0.5 C3A H:HEM301 4.4 32.6 0.5 C2C H:HEM301 4.4 51.0 0.5 CB G:MET52 4.4 44.5 1.0 C2B H:HEM301 4.4 32.3 0.5 C2C H:HEM301 4.4 32.1 0.5 C2A H:HEM301 4.4 33.7 0.5 C3A H:HEM301 4.4 51.7 0.5 C2B H:HEM301 4.5 50.9 0.5

Iron binding site 8 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe301 b:51.0 occ:0.50 FE H:HEM301 0.0 51.0 0.5 FE H:HEM301 0.1 31.8 0.5 NC H:HEM301 2.0 31.0 0.5 ND H:HEM301 2.0 31.7 0.5 NA H:HEM301 2.1 51.1 0.5 ND H:HEM301 2.1 51.2 0.5 NB H:HEM301 2.1 50.5 0.5 NC H:HEM301 2.1 50.8 0.5 NB H:HEM301 2.1 31.3 0.5 NA H:HEM301 2.2 32.2 0.5 SD H:MET52 2.4 44.4 1.0 SD G:MET52 2.6 43.3 1.0 C4C H:HEM301 3.0 31.4 0.5 C1D H:HEM301 3.0 31.7 0.5 C1C H:HEM301 3.0 31.0 0.5 C1A H:HEM301 3.1 52.3 0.5 C4D H:HEM301 3.1 33.5 0.5 C4D H:HEM301 3.1 52.2 0.5 C1C H:HEM301 3.1 50.3 0.5 C4B H:HEM301 3.1 50.6 0.5 C4B H:HEM301 3.1 30.9 0.5 C1D H:HEM301 3.1 51.5 0.5 C1B H:HEM301 3.1 50.8 0.5 C4A H:HEM301 3.1 51.0 0.5 C4C H:HEM301 3.1 51.0 0.5 C1B H:HEM301 3.2 31.9 0.5 C4A H:HEM301 3.2 32.5 0.5 C1A H:HEM301 3.2 33.5 0.5 CHD H:HEM301 3.4 32.7 0.5 CE H:MET52 3.4 44.2 1.0 CHC H:HEM301 3.4 31.1 0.5 CHC H:HEM301 3.4 50.5 0.5 CHA H:HEM301 3.4 52.1 0.5 CG H:MET52 3.4 43.2 1.0 CHB H:HEM301 3.5 51.4 0.5 CHD H:HEM301 3.5 51.7 0.5 CHA H:HEM301 3.5 33.2 0.5 CHB H:HEM301 3.5 32.4 0.5 CG G:MET52 3.6 43.2 1.0 CE G:MET52 3.6 44.4 1.0 C3C H:HEM301 4.3 31.7 0.5 C3D H:HEM301 4.3 33.6 0.5 C3B H:HEM301 4.3 51.1 0.5 C3B H:HEM301 4.3 31.6 0.5 C3D H:HEM301 4.3 52.5 0.5 C2D H:HEM301 4.3 32.9 0.5 C2C H:HEM301 4.3 32.1 0.5 C2D H:HEM301 4.4 51.8 0.5 C2A H:HEM301 4.4 52.2 0.5 C3C H:HEM301 4.4 50.8 0.5 CB G:MET52 4.4 44.5 1.0 C2B H:HEM301 4.4 50.9 0.5 CB H:MET52 4.4 43.5 1.0 C2C H:HEM301 4.4 51.0 0.5 C3A H:HEM301 4.4 51.7 0.5 C2B H:HEM301 4.4 32.3 0.5 C3A H:HEM301 4.5 32.6 0.5 C2A H:HEM301 4.5 33.7 0.5

Iron binding site 9 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe301 b:43.7 occ:0.50 FE I:HEM301 0.0 43.7 0.5 FE I:HEM301 0.1 57.2 0.5 NC I:HEM301 2.0 56.4 0.5 NA I:HEM301 2.1 44.2 0.5 ND I:HEM301 2.1 57.6 0.5 ND I:HEM301 2.1 43.5 0.5 NC I:HEM301 2.1 44.0 0.5 NB I:HEM301 2.1 42.6 0.5 NB I:HEM301 2.1 57.4 0.5 NA I:HEM301 2.1 57.0 0.5 SD I:MET52 2.3 45.1 1.0 SD J:MET52 2.5 43.8 1.0 C4C I:HEM301 3.0 56.6 0.5 C4B I:HEM301 3.1 57.4 0.5 C1D I:HEM301 3.1 57.7 0.5 C4C I:HEM301 3.1 44.6 0.5 C1C I:HEM301 3.1 56.3 0.5 C1A I:HEM301 3.1 44.3 0.5 C4B I:HEM301 3.1 42.5 0.5 C4A I:HEM301 3.1 44.3 0.5 C4D I:HEM301 3.1 44.6 0.5 C1D I:HEM301 3.1 43.4 0.5 C1B I:HEM301 3.1 43.0 0.5 C1A I:HEM301 3.1 57.8 0.5 C1C I:HEM301 3.1 43.9 0.5 C4D I:HEM301 3.1 57.7 0.5 C1B I:HEM301 3.1 57.8 0.5 C4A I:HEM301 3.1 57.0 0.5 CE I:MET52 3.3 44.1 1.0 CHA I:HEM301 3.4 44.5 0.5 CHD I:HEM301 3.4 57.4 0.5 CHC I:HEM301 3.4 56.9 0.5 CHA I:HEM301 3.4 57.8 0.5 CHC I:HEM301 3.4 43.2 0.5 CHB I:HEM301 3.5 43.9 0.5 CHD I:HEM301 3.5 44.5 0.5 CHB I:HEM301 3.5 57.7 0.5 CG J:MET52 3.5 43.8 1.0 CG I:MET52 3.6 43.7 1.0 CE J:MET52 3.6 43.8 1.0 C3B I:HEM301 4.3 57.6 0.5 C3B I:HEM301 4.3 43.0 0.5 CB I:MET52 4.3 43.6 1.0 C3D I:HEM301 4.3 44.8 0.5 C3D I:HEM301 4.3 58.0 0.5 C3C I:HEM301 4.3 56.8 0.5 C3C I:HEM301 4.3 44.2 0.5 C2D I:HEM301 4.4 57.5 0.5 C2D I:HEM301 4.4 43.7 0.5 C2C I:HEM301 4.4 56.8 0.5 C2A I:HEM301 4.4 44.7 0.5 C3A I:HEM301 4.4 44.1 0.5 C2B I:HEM301 4.4 57.6 0.5 C2B I:HEM301 4.4 43.2 0.5 C2C I:HEM301 4.4 44.3 0.5 C2A I:HEM301 4.4 58.0 0.5 C3A I:HEM301 4.4 57.2 0.5 CB J:MET52 4.4 43.9 1.0

Iron binding site 10 out of 12 in the The Structure of Mycobacterial Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of The Structure of Mycobacterial Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe301 b:57.2 occ:0.50 FE I:HEM301 0.0 57.2 0.5 FE I:HEM301 0.1 43.7 0.5 ND I:HEM301 2.0 43.5 0.5 NC I:HEM301 2.1 44.0 0.5 NB I:HEM301 2.1 57.4 0.5 NA I:HEM301 2.1 57.0 0.5 ND I:HEM301 2.1 57.6 0.5 NA I:HEM301 2.1 44.2 0.5 NC I:HEM301 2.1 56.4 0.5 NB I:HEM301 2.1 42.6 0.5 SD I:MET52 2.3 45.1 1.0 SD J:MET52 2.4 43.8 1.0 C4C I:HEM301 3.1 44.6 0.5 C4D I:HEM301 3.1 44.6 0.5 C1D I:HEM301 3.1 43.4 0.5 C1A I:HEM301 3.1 57.8 0.5 C1A I:HEM301 3.1 44.3 0.5 C4C I:HEM301 3.1 56.6 0.5 C4B I:HEM301 3.1 57.4 0.5 C1D I:HEM301 3.1 57.7 0.5 C1B I:HEM301 3.1 57.8 0.5 C4D I:HEM301 3.1 57.7 0.5 C4A I:HEM301 3.1 57.0 0.5 C4A I:HEM301 3.1 44.3 0.5 C1C I:HEM301 3.1 56.3 0.5 C1C I:HEM301 3.1 43.9 0.5 C4B I:HEM301 3.1 42.5 0.5 C1B I:HEM301 3.1 43.0 0.5 CE I:MET52 3.4 44.1 1.0 CHA I:HEM301 3.4 44.5 0.5 CHA I:HEM301 3.4 57.8 0.5 CHD I:HEM301 3.4 44.5 0.5 CHC I:HEM301 3.4 56.9 0.5 CHD I:HEM301 3.4 57.4 0.5 CHC I:HEM301 3.5 43.2 0.5 CHB I:HEM301 3.5 57.7 0.5 CG J:MET52 3.5 43.8 1.0 CHB I:HEM301 3.5 43.9 0.5 CE J:MET52 3.6 43.8 1.0 CG I:MET52 3.6 43.7 1.0 C3B I:HEM301 4.3 57.6 0.5 C3D I:HEM301 4.3 44.8 0.5 C3B I:HEM301 4.3 43.0 0.5 CB I:MET52 4.3 43.6 1.0 C3D I:HEM301 4.3 58.0 0.5 C2D I:HEM301 4.3 43.7 0.5 C3C I:HEM301 4.3 44.2 0.5 C3C I:HEM301 4.4 56.8 0.5 C2D I:HEM301 4.4 57.5 0.5 C2A I:HEM301 4.4 44.7 0.5 C2A I:HEM301 4.4 58.0 0.5 C2B I:HEM301 4.4 57.6 0.5 C3A I:HEM301 4.4 44.1 0.5 C3A I:HEM301 4.4 57.2 0.5 C2C I:HEM301 4.4 44.3 0.5 C2C I:HEM301 4.4 56.8 0.5 CB J:MET52 4.4 43.9 1.0 C2B I:HEM301 4.4 43.2 0.5

R.Janowski, T.Auerbach-Nevo, M.S.Weiss. Bacterioferritin From Mycobacterium Smegmatis Contains Zinc in Its Di-Nuclear Site. Protein Sci. V. 17 1138 2008.
ISSN: ISSN 0961-8368
PubMed: 18445621
DOI: 10.1110/PS.034819.108