Iron in PDB 6k3o: Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor

All present enzymatic activity of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor:
1.16.3.1;

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 36;

Binding sites:

The binding sites of Iron atom in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor (pdb code 6k3o). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 36 binding sites of Iron where determined in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor, PDB code: 6k3o:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:80.4 occ:1.00 OE2 A:GLU18 2.1 61.0 1.0 OE1 A:GLU51 2.1 61.7 1.0 OE2 A:GLU51 2.1 61.7 1.0 OE1 A:GLU18 2.1 61.0 1.0 OE2 A:GLU127 2.1 64.5 1.0 CD A:GLU51 2.3 61.7 1.0 ND1 A:HIS54 2.4 61.1 1.0 CD A:GLU18 2.4 61.0 1.0 CE1 A:HIS54 3.2 61.1 1.0 CD A:GLU127 3.4 64.5 1.0 CG A:HIS54 3.4 61.1 1.0 CB A:HIS54 3.8 61.1 1.0 CG A:GLU51 3.8 61.7 1.0 CG A:GLU18 3.9 61.0 1.0 OE1 A:GLU127 4.1 64.5 1.0 NE2 A:HIS54 4.4 61.1 1.0 CG A:GLU127 4.5 64.5 1.0 CD2 A:HIS54 4.5 61.1 1.0 CA A:GLU51 4.5 61.7 1.0 CB A:GLU51 4.6 61.7 1.0 CB A:GLU18 4.8 61.0 1.0 CG2 A:ILE123 4.8 62.4 1.0

Iron binding site 2 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:61.5 occ:1.00 FE B:HEM201 0.0 61.5 1.0 NC B:HEM201 2.0 61.5 1.0 NA B:HEM201 2.0 61.5 1.0 NB B:HEM201 2.0 61.5 1.0 ND B:HEM201 2.1 61.5 1.0 CE A:MET52 2.1 61.4 1.0 SD B:MET52 2.4 61.5 1.0 C1B B:HEM201 3.0 61.5 1.0 C4A B:HEM201 3.0 61.5 1.0 C4B B:HEM201 3.0 61.5 1.0 C1A B:HEM201 3.0 61.5 1.0 C1C B:HEM201 3.1 61.5 1.0 C4C B:HEM201 3.1 61.5 1.0 C4D B:HEM201 3.1 61.5 1.0 C1D B:HEM201 3.1 61.5 1.0 CE B:MET52 3.3 61.5 1.0 CHB B:HEM201 3.4 61.5 1.0 CHC B:HEM201 3.4 61.5 1.0 CHA B:HEM201 3.4 61.5 1.0 CHD B:HEM201 3.4 61.5 1.0 SD A:MET52 3.5 61.4 1.0 CG B:MET52 4.1 61.5 1.0 C2B B:HEM201 4.2 61.5 1.0 C3B B:HEM201 4.2 61.5 1.0 C3A B:HEM201 4.2 61.5 1.0 C2A B:HEM201 4.2 61.5 1.0 C2C B:HEM201 4.3 61.5 1.0 C3C B:HEM201 4.3 61.5 1.0 C3D B:HEM201 4.3 61.5 1.0 C2D B:HEM201 4.3 61.5 1.0 CG A:MET52 4.9 61.4 1.0

Iron binding site 3 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:80.3 occ:1.00 OE1 B:GLU18 2.1 61.6 1.0 OE1 B:GLU51 2.1 62.2 1.0 OE2 B:GLU51 2.1 62.2 1.0 OE2 B:GLU18 2.1 61.6 1.0 OE1 B:GLU127 2.1 65.4 1.0 CD B:GLU51 2.3 62.2 1.0 ND1 B:HIS54 2.3 61.6 1.0 CD B:GLU18 2.4 61.6 1.0 CE1 B:HIS54 3.2 61.6 1.0 CD B:GLU127 3.4 65.4 1.0 CG B:HIS54 3.4 61.6 1.0 CB B:HIS54 3.7 61.6 1.0 CG B:GLU51 3.8 62.2 1.0 CG B:GLU18 3.9 61.6 1.0 OE2 B:GLU127 4.1 65.4 1.0 NE2 B:HIS54 4.4 61.6 1.0 CG B:GLU127 4.4 65.4 1.0 CA B:GLU51 4.4 62.2 1.0 CD2 B:HIS54 4.5 61.6 1.0 CB B:GLU51 4.5 62.2 1.0 CB B:GLU18 4.8 61.6 1.0 CG2 B:ILE123 4.8 62.6 1.0 O B:GLU51 5.0 62.2 1.0

Iron binding site 4 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:79.8 occ:1.00 OE2 C:GLU18 2.1 61.4 1.0 OE2 C:GLU51 2.1 62.6 1.0 OE1 C:GLU51 2.1 62.6 1.0 OE1 C:GLU18 2.1 61.4 1.0 OE2 C:GLU127 2.2 65.2 1.0 CD C:GLU51 2.3 62.6 1.0 CD C:GLU18 2.4 61.4 1.0 ND1 C:HIS54 2.4 62.2 1.0 CE1 C:HIS54 3.2 62.2 1.0 CD C:GLU127 3.4 65.2 1.0 CG C:HIS54 3.5 62.2 1.0 CG C:GLU51 3.8 62.6 1.0 CB C:HIS54 3.8 62.2 1.0 CG C:GLU18 3.9 61.4 1.0 OE1 C:GLU127 4.1 65.2 1.0 NE2 C:HIS54 4.4 62.2 1.0 CG C:GLU127 4.5 65.2 1.0 CD2 C:HIS54 4.5 62.2 1.0 CA C:GLU51 4.6 62.6 1.0 CB C:GLU51 4.6 62.6 1.0 CG2 C:ILE123 4.7 63.6 1.0 CB C:GLU18 4.8 61.4 1.0

Iron binding site 5 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe202 b:64.3 occ:1.00 FE C:HEM202 0.0 64.3 1.0 NB C:HEM202 2.1 64.3 1.0 NA C:HEM202 2.1 64.3 1.0 ND C:HEM202 2.1 64.3 1.0 NC C:HEM202 2.1 64.3 1.0 CE C:MET52 2.1 63.0 1.0 SD C:MET52 2.8 63.0 1.0 C1C C:HEM202 3.0 64.3 1.0 C4C C:HEM202 3.0 64.3 1.0 CE D:MET52 3.0 61.5 1.0 C1A C:HEM202 3.0 64.3 1.0 C4A C:HEM202 3.0 64.3 1.0 C4B C:HEM202 3.0 64.3 1.0 C1B C:HEM202 3.1 64.3 1.0 C4D C:HEM202 3.1 64.3 1.0 C1D C:HEM202 3.1 64.3 1.0 CHC C:HEM202 3.4 64.3 1.0 CHA C:HEM202 3.4 64.3 1.0 CHD C:HEM202 3.4 64.3 1.0 CHB C:HEM202 3.4 64.3 1.0 SD D:MET52 3.7 61.5 1.0 C2C C:HEM202 4.1 64.3 1.0 C3C C:HEM202 4.1 64.3 1.0 C2A C:HEM202 4.2 64.3 1.0 C3A C:HEM202 4.2 64.3 1.0 C3B C:HEM202 4.3 64.3 1.0 C2B C:HEM202 4.3 64.3 1.0 C2D C:HEM202 4.3 64.3 1.0 C3D C:HEM202 4.3 64.3 1.0 CG C:MET52 4.5 63.0 1.0 CE1 C:PHE49 5.0 60.5 1.0

Iron binding site 6 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:80.8 occ:1.00 OE2 D:GLU18 2.1 61.5 1.0 OE1 D:GLU51 2.1 62.7 1.0 OE2 D:GLU51 2.1 62.7 1.0 OE1 D:GLU18 2.1 61.5 1.0 OE2 D:GLU127 2.1 66.3 1.0 CD D:GLU51 2.3 62.7 1.0 ND1 D:HIS54 2.3 61.6 1.0 CD D:GLU18 2.4 61.5 1.0 CE1 D:HIS54 3.2 61.6 1.0 CD D:GLU127 3.4 66.3 1.0 CG D:HIS54 3.4 61.6 1.0 CB D:HIS54 3.7 61.6 1.0 CG D:GLU51 3.8 62.7 1.0 CG D:GLU18 3.9 61.5 1.0 OE1 D:GLU127 4.1 66.3 1.0 NE2 D:HIS54 4.4 61.6 1.0 CG D:GLU127 4.4 66.3 1.0 CD2 D:HIS54 4.5 61.6 1.0 CA D:GLU51 4.5 62.7 1.0 CB D:GLU51 4.6 62.7 1.0 CB D:GLU18 4.7 61.5 1.0 CG2 D:ILE123 4.8 63.0 1.0

Iron binding site 7 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe201 b:78.0 occ:1.00 OE2 F:GLU18 2.1 59.9 1.0 OE2 F:GLU51 2.1 60.4 1.0 OE1 F:GLU51 2.1 60.4 1.0 OE1 F:GLU18 2.1 59.9 1.0 OE2 F:GLU127 2.2 64.6 1.0 CD F:GLU51 2.3 60.4 1.0 ND1 F:HIS54 2.4 60.3 1.0 CD F:GLU18 2.4 59.9 1.0 CE1 F:HIS54 3.2 60.3 1.0 CD F:GLU127 3.4 64.6 1.0 CG F:HIS54 3.4 60.3 1.0 CB F:HIS54 3.8 60.3 1.0 CG F:GLU51 3.8 60.4 1.0 CG F:GLU18 3.9 59.9 1.0 OE1 F:GLU127 4.1 64.6 1.0 NE2 F:HIS54 4.4 60.3 1.0 CG F:GLU127 4.5 64.6 1.0 CD2 F:HIS54 4.5 60.3 1.0 CA F:GLU51 4.6 60.4 1.0 CB F:GLU51 4.6 60.4 1.0 CB F:GLU18 4.8 59.9 1.0 CG2 F:ILE123 4.8 62.3 1.0

Iron binding site 8 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe202 b:59.1 occ:1.00 FE F:HEM202 0.0 59.1 1.0 NC F:HEM202 2.0 59.1 1.0 ND F:HEM202 2.0 59.1 1.0 NB F:HEM202 2.0 59.1 1.0 NA F:HEM202 2.1 59.1 1.0 CE F:MET52 2.8 59.3 1.0 SD F:MET52 2.8 59.3 1.0 SD E:MET52 2.9 58.6 1.0 C1D F:HEM202 3.0 59.1 1.0 C4D F:HEM202 3.0 59.1 1.0 C4A F:HEM202 3.0 59.1 1.0 C4C F:HEM202 3.0 59.1 1.0 C1B F:HEM202 3.1 59.1 1.0 C1A F:HEM202 3.1 59.1 1.0 C1C F:HEM202 3.1 59.1 1.0 C4B F:HEM202 3.1 59.1 1.0 CE E:MET52 3.1 58.6 1.0 CHD F:HEM202 3.4 59.1 1.0 CHB F:HEM202 3.4 59.1 1.0 CHA F:HEM202 3.4 59.1 1.0 CHC F:HEM202 3.4 59.1 1.0 CG F:MET52 4.0 59.3 1.0 C2D F:HEM202 4.2 59.1 1.0 C3D F:HEM202 4.2 59.1 1.0 CG E:MET52 4.2 58.6 1.0 C3A F:HEM202 4.2 59.1 1.0 C2A F:HEM202 4.3 59.1 1.0 C3C F:HEM202 4.3 59.1 1.0 C2C F:HEM202 4.3 59.1 1.0 C2B F:HEM202 4.3 59.1 1.0 C3B F:HEM202 4.3 59.1 1.0 CB E:MET52 4.9 58.6 1.0

Iron binding site 9 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:78.5 occ:1.00 OE2 E:GLU18 2.1 59.7 1.0 OE1 E:GLU51 2.1 60.0 1.0 OE2 E:GLU51 2.1 60.0 1.0 OE1 E:GLU18 2.1 59.7 1.0 OE2 E:GLU127 2.2 65.4 1.0 CD E:GLU51 2.3 60.0 1.0 ND1 E:HIS54 2.4 59.5 1.0 CD E:GLU18 2.4 59.7 1.0 CE1 E:HIS54 3.2 59.5 1.0 CD E:GLU127 3.4 65.4 1.0 CG E:HIS54 3.4 59.5 1.0 CB E:HIS54 3.8 59.5 1.0 CG E:GLU51 3.8 60.0 1.0 CG E:GLU18 3.9 59.7 1.0 OE1 E:GLU127 4.1 65.4 1.0 NE2 E:HIS54 4.4 59.5 1.0 CG E:GLU127 4.5 65.4 1.0 CD2 E:HIS54 4.5 59.5 1.0 CA E:GLU51 4.5 60.0 1.0 CB E:GLU51 4.6 60.0 1.0 CB E:GLU18 4.8 59.7 1.0 CG2 E:ILE123 4.8 63.8 1.0

Iron binding site 10 out of 36 in the Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe201 b:79.3 occ:1.00 OE2 G:GLU18 2.1 60.4 1.0 OE1 G:GLU51 2.1 61.0 1.0 OE2 G:GLU51 2.1 61.0 1.0 OE1 G:GLU18 2.1 60.4 1.0 OE2 G:GLU127 2.1 66.0 1.0 CD G:GLU51 2.3 61.0 1.0 ND1 G:HIS54 2.3 60.1 1.0 CD G:GLU18 2.4 60.4 1.0 CE1 G:HIS54 3.2 60.1 1.0 CD G:GLU127 3.4 66.0 1.0 CG G:HIS54 3.4 60.1 1.0 CB G:HIS54 3.7 60.1 1.0 CG G:GLU51 3.8 61.0 1.0 CG G:GLU18 3.9 60.4 1.0 OE1 G:GLU127 4.1 66.0 1.0 NE2 G:HIS54 4.4 60.1 1.0 CG G:GLU127 4.4 66.0 1.0 CD2 G:HIS54 4.5 60.1 1.0 CA G:GLU51 4.5 61.0 1.0 CB G:GLU51 4.6 61.0 1.0 CB G:GLU18 4.7 60.4 1.0 CG2 G:ILE123 4.8 63.6 1.0

C.Jobichen, J.Sivaraman. Cryo-Em Structure of Apo-Bacterioferritin From Streptomyces Coelicolor To Be Published.