Iron in PDB 8jb0: Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry

All present enzymatic activity of Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry:
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 Holo Form of Scbfr in C1 Symmetry (pdb code 8jb0). 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 Holo Form of Scbfr in C1 Symmetry, PDB code: 8jb0:
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 Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:160.3 occ:1.00 OE2 A:GLU127 2.7 127.5 1.0 OE1 A:GLU18 2.7 117.1 1.0 OE2 A:GLU18 2.8 117.1 1.0 OE1 A:GLU51 2.8 117.9 1.0 ND1 A:HIS54 2.9 116.4 1.0 CD A:GLU127 3.0 127.5 1.0 CD A:GLU18 3.1 117.1 1.0 OE2 A:GLU51 3.1 117.9 1.0 CD A:GLU51 3.3 117.9 1.0 CG2 A:ILE123 3.5 122.7 1.0 CG A:GLU127 3.5 127.5 1.0 OE1 A:GLU127 3.6 127.5 1.0 CE1 A:HIS54 3.7 116.4 1.0 CG A:HIS54 3.9 116.4 1.0 CB A:HIS54 4.1 116.4 1.0 CG A:GLU18 4.6 117.1 1.0 NE2 A:GLN14 4.7 113.8 1.0 CB A:ILE123 4.7 122.7 1.0 CG A:GLU51 4.8 117.9 1.0 NE2 A:HIS54 4.9 116.4 1.0 CD2 A:HIS54 4.9 116.4 1.0 O A:ILE123 4.9 122.7 1.0 CB A:GLU127 5.0 127.5 1.0

Iron binding site 2 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:119.2 occ:1.00 SD A:MET52 3.1 113.8 1.0 CE1 A:PHE49 3.1 110.4 1.0 CD1 A:PHE49 3.1 110.4 1.0 CE B:MET52 3.2 100.0 1.0 CZ A:PHE49 4.2 110.4 1.0 OG A:SER48 4.2 108.7 1.0 CG A:PHE49 4.2 110.4 1.0 CB A:MET52 4.4 113.8 1.0 CG A:MET52 4.4 113.8 1.0 SD B:MET52 4.4 100.0 1.0 CE A:MET52 4.4 113.8 1.0 CA A:PHE49 4.5 110.4 1.0 O A:SER48 4.7 108.7 1.0 N A:PHE49 4.8 110.4 1.0 CE2 A:PHE26 4.8 112.7 1.0 CD2 A:PHE26 4.8 112.7 1.0 C A:SER48 4.9 108.7 1.0 CB A:PHE49 5.0 110.4 1.0

Iron binding site 3 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:150.0 occ:1.00 OE2 B:GLU127 2.8 115.9 1.0 OE1 B:GLU51 2.8 103.0 1.0 CD B:GLU51 3.6 103.0 1.0 CD B:GLU127 3.7 115.9 1.0 OE2 B:GLU51 4.0 103.0 1.0 CG B:GLU18 4.0 99.8 1.0 OE1 B:GLU127 4.0 115.9 1.0 CA B:GLU18 4.1 99.8 1.0 CB B:GLU18 4.2 99.8 1.0 CB B:ALA21 4.2 97.2 1.0 NE2 B:GLN14 4.4 104.7 1.0 CD B:GLU18 4.8 99.8 1.0 OE2 B:GLU94 4.8 127.7 1.0 CG B:GLU51 4.8 103.0 1.0 CG B:GLU127 4.8 115.9 1.0 N B:GLU18 4.9 99.8 1.0

Iron binding site 4 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:149.2 occ:1.00 OE2 C:GLU51 2.9 125.7 1.0 OE2 C:GLU127 2.9 144.0 1.0 CD C:GLU127 3.2 144.0 1.0 OE2 C:GLU18 3.3 119.6 1.0 CG C:GLU18 3.3 119.6 1.0 CG2 C:ILE123 3.3 131.1 1.0 CG C:GLU127 3.6 144.0 1.0 CD C:GLU18 3.8 119.6 1.0 CD C:GLU51 3.8 125.7 1.0 ND1 C:HIS54 3.8 124.3 1.0 OE1 C:GLU127 4.0 144.0 1.0 OE1 C:GLU51 4.0 125.7 1.0 CB C:HIS54 4.5 124.3 1.0 CG C:HIS54 4.5 124.3 1.0 CE1 C:HIS54 4.7 124.3 1.0 CB C:GLU18 4.7 119.6 1.0 CB C:ILE123 4.8 131.1 1.0 CD1 C:ILE123 4.9 131.1 1.0 NE2 C:GLN14 4.9 115.9 1.0 OE1 C:GLU18 5.0 119.6 1.0

Iron binding site 5 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe202 b:140.0 occ:1.00 SD D:MET52 3.2 104.4 1.0 CE1 C:PHE49 3.3 107.8 1.0 CE D:MET52 3.7 104.4 1.0 CZ C:PHE49 3.7 107.8 1.0 SD C:MET52 4.2 111.7 1.0 CD1 C:PHE49 4.2 107.8 1.0 CG D:MET52 4.6 104.4 1.0 CE C:MET52 4.7 111.7 1.0 CE2 C:PHE49 4.8 107.8 1.0

Iron binding site 6 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:169.0 occ:1.00 OE2 D:GLU18 2.7 112.6 1.0 OE1 D:GLU51 2.7 119.8 1.0 OE1 D:GLU127 2.9 148.0 1.0 CD D:GLU127 2.9 148.0 1.0 OE1 D:GLU18 2.9 112.6 1.0 CD D:GLU18 3.2 112.6 1.0 OE2 D:GLU127 3.2 148.0 1.0 CD D:GLU51 3.6 119.8 1.0 CG D:GLU127 3.6 148.0 1.0 OE2 D:GLU51 3.6 119.8 1.0 CG2 D:ILE123 4.3 153.7 1.0 CD2 D:HIS54 4.3 124.0 1.0 CG D:GLU18 4.7 112.6 1.0 CB D:GLU127 4.9 148.0 1.0 NE2 D:GLN14 5.0 120.1 1.0 CG D:GLU51 5.0 119.8 1.0 CB D:ALA97 5.0 129.5 1.0 OE1 D:GLU94 5.0 135.7 1.0

Iron binding site 7 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe201 b:193.8 occ:1.00 OE2 F:GLU47 2.9 124.9 1.0 OE1 F:GLU127 2.9 152.7 1.0 O F:ASP126 3.0 156.9 1.0 C F:ASP126 3.1 156.9 1.0 CD F:GLU127 3.2 152.7 1.0 N F:GLU127 3.3 152.7 1.0 OE2 F:GLU127 3.3 152.7 1.0 OE2 F:GLU51 3.3 121.1 1.0 CA F:GLU127 3.5 152.7 1.0 CB F:ASP126 3.6 156.9 1.0 CB F:HIS130 3.7 131.0 1.0 CE1 F:HIS54 3.9 132.2 1.0 CA F:ASP126 3.9 156.9 1.0 CD F:GLU47 4.0 124.9 1.0 CG F:GLU127 4.1 152.7 1.0 CB F:GLU127 4.3 152.7 1.0 OE1 F:GLU47 4.4 124.9 1.0 CG F:HIS130 4.4 131.0 1.0 CG F:ASP126 4.5 156.9 1.0 CD F:GLU51 4.6 121.1 1.0 C F:GLU127 4.6 152.7 1.0 ND1 F:HIS54 4.6 132.2 1.0 CD2 F:HIS130 4.6 131.0 1.0 N F:HIS130 4.8 131.0 1.0 CA F:HIS130 4.9 131.0 1.0 NE2 F:HIS54 4.9 132.2 1.0 OD2 F:ASP126 4.9 156.9 1.0 O F:GLU127 5.0 152.7 1.0

Iron binding site 8 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:164.6 occ:1.00 CE E:MET52 3.2 113.0 1.0 SD F:MET52 3.4 113.9 1.0 CE1 F:PHE49 3.5 115.1 1.0 CE F:MET52 4.0 113.9 1.0 CD1 F:PHE49 4.0 115.1 1.0 SD E:MET52 4.0 113.0 1.0 CZ F:PHE49 4.2 115.1 1.0

Iron binding site 9 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe202 b:150.5 occ:1.00 OE2 E:GLU18 2.7 133.6 1.0 OE2 E:GLU127 2.7 143.7 1.0 OE1 E:GLU18 3.0 133.6 1.0 OE1 E:GLU51 3.0 119.1 1.0 CD E:GLU127 3.0 143.7 1.0 CD E:GLU18 3.2 133.6 1.0 CD2 E:HIS54 3.2 125.3 1.0 CG E:GLU127 3.4 143.7 1.0 CG2 E:ILE123 3.4 145.4 1.0 OE2 E:GLU51 3.6 119.1 1.0 CD E:GLU51 3.7 119.1 1.0 OE1 E:GLU127 3.7 143.7 1.0 CG E:HIS54 3.9 125.3 1.0 NE2 E:HIS54 4.0 125.3 1.0 CB E:HIS54 4.2 125.3 1.0 O E:ILE123 4.4 145.4 1.0 CD1 E:ILE123 4.6 145.4 1.0 CG E:GLU18 4.6 133.6 1.0 CB E:ILE123 4.7 145.4 1.0 NE2 E:GLN14 4.8 132.4 1.0 ND1 E:HIS54 4.8 125.3 1.0 CB E:GLU127 4.9 143.7 1.0 CE1 E:HIS54 4.9 125.3 1.0 CA E:ILE123 5.0 145.4 1.0

Iron binding site 10 out of 36 in the Cryo-Em Structure of Holo Form of Scbfr in C1 Symmetry


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 Holo Form of Scbfr in C1 Symmetry within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe201 b:169.5 occ:1.00 OE1 G:GLU18 2.7 110.1 1.0 OE1 G:GLU51 2.8 113.0 1.0 OE2 G:GLU51 2.9 113.0 1.0 CD G:GLU127 2.9 126.5 1.0 OE2 G:GLU127 2.9 126.5 1.0 OE2 G:GLU18 3.1 110.1 1.0 CD G:GLU51 3.1 113.0 1.0 OE1 G:GLU127 3.2 126.5 1.0 CD G:GLU18 3.2 110.1 1.0 CG G:GLU127 3.4 126.5 1.0 ND1 G:HIS54 4.2 110.4 1.0 CG2 G:ILE123 4.4 124.6 1.0 CG G:GLU51 4.5 113.0 1.0 NE2 G:GLN14 4.7 113.2 1.0 CG G:GLU18 4.7 110.1 1.0 OE1 G:GLU94 4.8 126.9 1.0 CB G:GLU127 4.9 126.5 1.0 CE1 G:HIS54 4.9 110.4 1.0

C.Jobichen, T.Y.Chong, R.Rattinam, S.Basak, M.Srinivasan, Y.K.Choong, K.P.Pandey, T.B.Ngoc, J.Shi, J.Angayarkann, J.Sivaraman. Bacterioferritin Nanocage Structures Uncover the Bio-Mineralization Process in Ferritins PNAS Nexus 2023.
ISSN: ESSN 2752-6542
DOI: 10.1093/PNASNEXUS/PGAD235