Iron in PDB 9n5a: Cryoem Structure of Azotobacter Vinelandii Bacterioferritin

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin:
1.16.3.1;

Pages:

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

Binding sites:

The binding sites of Iron atom in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin (pdb code 9n5a). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin, PDB code: 9n5a:
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 Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe3001 b:50.0 occ:1.00 FE A:HEM3001 0.0 50.0 1.0 ND A:HEM3001 2.1 50.0 1.0 NA A:HEM3001 2.1 50.0 1.0 NC A:HEM3001 2.1 50.0 1.0 NB A:HEM3001 2.1 50.0 1.0 SD A:MET52 2.5 50.0 1.0 CG A:MET52 2.8 50.0 1.0 SD B:MET52 2.9 50.0 1.0 C1A A:HEM3001 3.1 50.0 1.0 C1C A:HEM3001 3.1 50.0 1.0 C4A A:HEM3001 3.1 50.0 1.0 C4D A:HEM3001 3.1 50.0 1.0 C1D A:HEM3001 3.1 50.0 1.0 C4B A:HEM3001 3.1 50.0 1.0 C1B A:HEM3001 3.1 50.0 1.0 C4C A:HEM3001 3.1 50.0 1.0 CE A:MET52 3.2 50.0 1.0 CHC A:HEM3001 3.4 50.0 1.0 CHA A:HEM3001 3.4 50.0 1.0 CHB A:HEM3001 3.5 50.0 1.0 CHD A:HEM3001 3.5 50.0 1.0 CB A:MET52 3.8 50.0 1.0 CE B:MET52 4.1 50.0 1.0 C3A A:HEM3001 4.3 50.0 1.0 C2A A:HEM3001 4.3 50.0 1.0 C3D A:HEM3001 4.3 50.0 1.0 C2C A:HEM3001 4.3 50.0 1.0 C2D A:HEM3001 4.3 50.0 1.0 C2B A:HEM3001 4.3 50.0 1.0 C3B A:HEM3001 4.3 50.0 1.0 C3C A:HEM3001 4.3 50.0 1.0 CG B:MET52 4.4 50.0 1.0 CB B:MET52 4.7 50.0 1.0 CD1 A:ILE49 5.0 50.0 1.0

Iron binding site 2 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:50.0 occ:1.00 FE D:HEM201 0.0 50.0 1.0 SD D:MET52 2.0 50.0 1.0 ND D:HEM201 2.1 50.0 1.0 NA D:HEM201 2.1 50.0 1.0 NC D:HEM201 2.1 50.0 1.0 NB D:HEM201 2.1 50.0 1.0 SD C:MET52 2.9 50.0 1.0 C4A D:HEM201 3.1 50.0 1.0 C1C D:HEM201 3.1 50.0 1.0 C4D D:HEM201 3.1 50.0 1.0 C1A D:HEM201 3.1 50.0 1.0 C1B D:HEM201 3.1 50.0 1.0 C1D D:HEM201 3.1 50.0 1.0 C4C D:HEM201 3.1 50.0 1.0 C4B D:HEM201 3.1 50.0 1.0 CE D:MET52 3.4 50.0 1.0 CHC D:HEM201 3.4 50.0 1.0 CHA D:HEM201 3.4 50.0 1.0 CHB D:HEM201 3.4 50.0 1.0 CHD D:HEM201 3.5 50.0 1.0 CG D:MET52 3.5 50.0 1.0 CB D:MET52 3.9 50.0 1.0 CG C:MET52 3.9 50.0 1.0 CE C:MET52 4.0 50.0 1.0 C3A D:HEM201 4.3 50.0 1.0 C2A D:HEM201 4.3 50.0 1.0 C3D D:HEM201 4.3 50.0 1.0 C2B D:HEM201 4.3 50.0 1.0 C2D D:HEM201 4.3 50.0 1.0 C2C D:HEM201 4.3 50.0 1.0 C3C D:HEM201 4.3 50.0 1.0 C3B D:HEM201 4.3 50.0 1.0 CB C:MET52 4.7 50.0 1.0 CD1 D:ILE49 4.8 50.0 1.0

Iron binding site 3 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:50.0 occ:1.00 FE E:HEM201 0.0 50.0 1.0 ND E:HEM201 2.1 50.0 1.0 NB E:HEM201 2.1 50.0 1.0 NA E:HEM201 2.1 50.0 1.0 NC E:HEM201 2.1 50.0 1.0 SD E:MET52 2.6 50.0 1.0 SD F:MET52 2.9 50.0 1.0 CG E:MET52 3.0 50.0 1.0 C4D E:HEM201 3.1 50.0 1.0 C4B E:HEM201 3.1 50.0 1.0 C1C E:HEM201 3.1 50.0 1.0 C1A E:HEM201 3.1 50.0 1.0 C1B E:HEM201 3.1 50.0 1.0 C1D E:HEM201 3.1 50.0 1.0 C4A E:HEM201 3.1 50.0 1.0 C4C E:HEM201 3.1 50.0 1.0 CE E:MET52 3.2 50.0 1.0 CHA E:HEM201 3.4 50.0 1.0 CHC E:HEM201 3.4 50.0 1.0 CHB E:HEM201 3.5 50.0 1.0 CHD E:HEM201 3.5 50.0 1.0 CB E:MET52 3.9 50.0 1.0 CE F:MET52 4.1 50.0 1.0 C3B E:HEM201 4.3 50.0 1.0 C3D E:HEM201 4.3 50.0 1.0 C2B E:HEM201 4.3 50.0 1.0 C2D E:HEM201 4.3 50.0 1.0 C2A E:HEM201 4.3 50.0 1.0 C3A E:HEM201 4.3 50.0 1.0 C2C E:HEM201 4.3 50.0 1.0 C3C E:HEM201 4.3 50.0 1.0 CG F:MET52 4.4 50.0 1.0 CB F:MET52 4.6 50.0 1.0

Iron binding site 4 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe201 b:50.0 occ:1.00 FE H:HEM201 0.0 50.0 1.0 ND H:HEM201 2.0 50.0 1.0 NB H:HEM201 2.0 50.0 1.0 NA H:HEM201 2.0 50.0 1.0 NC H:HEM201 2.0 50.0 1.0 SD H:MET52 2.2 50.0 1.0 C4D H:HEM201 3.1 50.0 1.0 C4B H:HEM201 3.1 50.0 1.0 C1C H:HEM201 3.1 50.0 1.0 C1A H:HEM201 3.1 50.0 1.0 C1D H:HEM201 3.1 50.0 1.0 C1B H:HEM201 3.1 50.0 1.0 C4A H:HEM201 3.1 50.0 1.0 C4C H:HEM201 3.1 50.0 1.0 SD G:MET52 3.1 50.0 1.0 CHA H:HEM201 3.4 50.0 1.0 CHC H:HEM201 3.4 50.0 1.0 CHB H:HEM201 3.4 50.0 1.0 CE H:MET52 3.4 50.0 1.0 CHD H:HEM201 3.4 50.0 1.0 CG G:MET52 3.5 50.0 1.0 CG H:MET52 3.8 50.0 1.0 CE G:MET52 3.8 50.0 1.0 CB H:MET52 4.2 50.0 1.0 CB G:MET52 4.2 50.0 1.0 C3D H:HEM201 4.3 50.0 1.0 C3B H:HEM201 4.3 50.0 1.0 C2D H:HEM201 4.3 50.0 1.0 C2A H:HEM201 4.3 50.0 1.0 C3A H:HEM201 4.3 50.0 1.0 C2B H:HEM201 4.3 50.0 1.0 C2C H:HEM201 4.3 50.0 1.0 C3C H:HEM201 4.3 50.0 1.0 CD1 H:ILE49 4.9 50.0 1.0

Iron binding site 5 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe3001 b:50.0 occ:1.00 FE I:HEM3001 0.0 50.0 1.0 NA I:HEM3001 2.1 50.0 1.0 ND I:HEM3001 2.1 50.0 1.0 NC I:HEM3001 2.1 50.0 1.0 NB I:HEM3001 2.1 50.0 1.0 SD I:MET52 2.5 50.0 1.0 CG I:MET52 2.8 50.0 1.0 SD J:MET52 2.9 50.0 1.0 C1A I:HEM3001 3.1 50.0 1.0 C1C I:HEM3001 3.1 50.0 1.0 C4A I:HEM3001 3.1 50.0 1.0 C4D I:HEM3001 3.1 50.0 1.0 C1D I:HEM3001 3.1 50.0 1.0 C4B I:HEM3001 3.1 50.0 1.0 C1B I:HEM3001 3.1 50.0 1.0 C4C I:HEM3001 3.1 50.0 1.0 CE I:MET52 3.2 50.0 1.0 CHC I:HEM3001 3.4 50.0 1.0 CHA I:HEM3001 3.4 50.0 1.0 CHB I:HEM3001 3.5 50.0 1.0 CHD I:HEM3001 3.5 50.0 1.0 CB I:MET52 3.8 50.0 1.0 CE J:MET52 4.1 50.0 1.0 C3A I:HEM3001 4.3 50.0 1.0 C2A I:HEM3001 4.3 50.0 1.0 C3D I:HEM3001 4.3 50.0 1.0 C2C I:HEM3001 4.3 50.0 1.0 C2D I:HEM3001 4.3 50.0 1.0 C2B I:HEM3001 4.3 50.0 1.0 C3B I:HEM3001 4.3 50.0 1.0 C3C I:HEM3001 4.3 50.0 1.0 CG J:MET52 4.4 50.0 1.0 CB J:MET52 4.7 50.0 1.0 CD1 I:ILE49 5.0 50.0 1.0

Iron binding site 6 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ L:Fe201 b:50.0 occ:1.00 FE L:HEM201 0.0 50.0 1.0 SD L:MET52 2.0 50.0 1.0 ND L:HEM201 2.1 50.0 1.0 NA L:HEM201 2.1 50.0 1.0 NC L:HEM201 2.1 50.0 1.0 NB L:HEM201 2.1 50.0 1.0 SD K:MET52 2.9 50.0 1.0 C4A L:HEM201 3.1 50.0 1.0 C4D L:HEM201 3.1 50.0 1.0 C1C L:HEM201 3.1 50.0 1.0 C1A L:HEM201 3.1 50.0 1.0 C1B L:HEM201 3.1 50.0 1.0 C1D L:HEM201 3.1 50.0 1.0 C4C L:HEM201 3.1 50.0 1.0 C4B L:HEM201 3.1 50.0 1.0 CE L:MET52 3.4 50.0 1.0 CHA L:HEM201 3.4 50.0 1.0 CHC L:HEM201 3.4 50.0 1.0 CHB L:HEM201 3.4 50.0 1.0 CHD L:HEM201 3.5 50.0 1.0 CG L:MET52 3.5 50.0 1.0 CB L:MET52 3.9 50.0 1.0 CG K:MET52 3.9 50.0 1.0 CE K:MET52 4.0 50.0 1.0 C3A L:HEM201 4.3 50.0 1.0 C2A L:HEM201 4.3 50.0 1.0 C3D L:HEM201 4.3 50.0 1.0 C2D L:HEM201 4.3 50.0 1.0 C2B L:HEM201 4.3 50.0 1.0 C2C L:HEM201 4.3 50.0 1.0 C3C L:HEM201 4.3 50.0 1.0 C3B L:HEM201 4.3 50.0 1.0 CB K:MET52 4.7 50.0 1.0 CD1 L:ILE49 4.8 50.0 1.0

Iron binding site 7 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe201 b:50.0 occ:1.00 FE M:HEM201 0.0 50.0 1.0 ND M:HEM201 2.1 50.0 1.0 NA M:HEM201 2.1 50.0 1.0 NB M:HEM201 2.1 50.0 1.0 NC M:HEM201 2.1 50.0 1.0 SD M:MET52 2.6 50.0 1.0 SD N:MET52 2.9 50.0 1.0 CG M:MET52 3.0 50.0 1.0 C4D M:HEM201 3.1 50.0 1.0 C4B M:HEM201 3.1 50.0 1.0 C1C M:HEM201 3.1 50.0 1.0 C1A M:HEM201 3.1 50.0 1.0 C1D M:HEM201 3.1 50.0 1.0 C1B M:HEM201 3.1 50.0 1.0 C4A M:HEM201 3.1 50.0 1.0 C4C M:HEM201 3.1 50.0 1.0 CE M:MET52 3.2 50.0 1.0 CHA M:HEM201 3.4 50.0 1.0 CHC M:HEM201 3.4 50.0 1.0 CHB M:HEM201 3.5 50.0 1.0 CHD M:HEM201 3.5 50.0 1.0 CB M:MET52 3.9 50.0 1.0 CE N:MET52 4.1 50.0 1.0 C3D M:HEM201 4.3 50.0 1.0 C3B M:HEM201 4.3 50.0 1.0 C2B M:HEM201 4.3 50.0 1.0 C2D M:HEM201 4.3 50.0 1.0 C2A M:HEM201 4.3 50.0 1.0 C3A M:HEM201 4.3 50.0 1.0 C2C M:HEM201 4.3 50.0 1.0 C3C M:HEM201 4.3 50.0 1.0 CG N:MET52 4.4 50.0 1.0 CB N:MET52 4.6 50.0 1.0

Iron binding site 8 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ P:Fe201 b:50.0 occ:1.00 FE P:HEM201 0.0 50.0 1.0 ND P:HEM201 2.0 50.0 1.0 NB P:HEM201 2.0 50.0 1.0 NA P:HEM201 2.0 50.0 1.0 NC P:HEM201 2.0 50.0 1.0 SD P:MET52 2.2 50.0 1.0 C4D P:HEM201 3.1 50.0 1.0 C4B P:HEM201 3.1 50.0 1.0 C1C P:HEM201 3.1 50.0 1.0 C1A P:HEM201 3.1 50.0 1.0 C1D P:HEM201 3.1 50.0 1.0 C4A P:HEM201 3.1 50.0 1.0 C1B P:HEM201 3.1 50.0 1.0 C4C P:HEM201 3.1 50.0 1.0 SD O:MET52 3.1 50.0 1.0 CE P:MET52 3.4 50.0 1.0 CHA P:HEM201 3.4 50.0 1.0 CHC P:HEM201 3.4 50.0 1.0 CHB P:HEM201 3.4 50.0 1.0 CHD P:HEM201 3.4 50.0 1.0 CG O:MET52 3.5 50.0 1.0 CG P:MET52 3.8 50.0 1.0 CE O:MET52 3.9 50.0 1.0 CB P:MET52 4.2 50.0 1.0 CB O:MET52 4.2 50.0 1.0 C3D P:HEM201 4.3 50.0 1.0 C3B P:HEM201 4.3 50.0 1.0 C2D P:HEM201 4.3 50.0 1.0 C2A P:HEM201 4.3 50.0 1.0 C3A P:HEM201 4.3 50.0 1.0 C2B P:HEM201 4.3 50.0 1.0 C2C P:HEM201 4.3 50.0 1.0 C3C P:HEM201 4.3 50.0 1.0 CD1 P:ILE49 4.9 50.0 1.0

Iron binding site 9 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ Q:Fe3001 b:50.0 occ:1.00 FE Q:HEM3001 0.0 50.0 1.0 ND Q:HEM3001 2.1 50.0 1.0 NA Q:HEM3001 2.1 50.0 1.0 NC Q:HEM3001 2.1 50.0 1.0 NB Q:HEM3001 2.1 50.0 1.0 SD Q:MET52 2.5 50.0 1.0 CG Q:MET52 2.8 50.0 1.0 SD R:MET52 2.9 50.0 1.0 C1A Q:HEM3001 3.1 50.0 1.0 C1C Q:HEM3001 3.1 50.0 1.0 C4A Q:HEM3001 3.1 50.0 1.0 C4D Q:HEM3001 3.1 50.0 1.0 C1D Q:HEM3001 3.1 50.0 1.0 C4B Q:HEM3001 3.1 50.0 1.0 C1B Q:HEM3001 3.1 50.0 1.0 C4C Q:HEM3001 3.1 50.0 1.0 CE Q:MET52 3.2 50.0 1.0 CHC Q:HEM3001 3.4 50.0 1.0 CHA Q:HEM3001 3.4 50.0 1.0 CHB Q:HEM3001 3.5 50.0 1.0 CHD Q:HEM3001 3.5 50.0 1.0 CB Q:MET52 3.8 50.0 1.0 CE R:MET52 4.1 50.0 1.0 C3A Q:HEM3001 4.3 50.0 1.0 C2A Q:HEM3001 4.3 50.0 1.0 C3D Q:HEM3001 4.3 50.0 1.0 C2C Q:HEM3001 4.3 50.0 1.0 C2D Q:HEM3001 4.3 50.0 1.0 C2B Q:HEM3001 4.3 50.0 1.0 C3B Q:HEM3001 4.3 50.0 1.0 C3C Q:HEM3001 4.3 50.0 1.0 CG R:MET52 4.4 50.0 1.0 CB R:MET52 4.7 50.0 1.0 CD1 Q:ILE49 5.0 50.0 1.0

Iron binding site 10 out of 12 in the Cryoem Structure of Azotobacter Vinelandii Bacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryoem Structure of Azotobacter Vinelandii Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ T:Fe201 b:50.0 occ:1.00 FE T:HEM201 0.0 50.0 1.0 SD T:MET52 2.0 50.0 1.0 ND T:HEM201 2.1 50.0 1.0 NA T:HEM201 2.1 50.0 1.0 NC T:HEM201 2.1 50.0 1.0 NB T:HEM201 2.1 50.0 1.0 SD S:MET52 2.9 50.0 1.0 C4A T:HEM201 3.1 50.0 1.0 C4D T:HEM201 3.1 50.0 1.0 C1C T:HEM201 3.1 50.0 1.0 C1A T:HEM201 3.1 50.0 1.0 C1B T:HEM201 3.1 50.0 1.0 C1D T:HEM201 3.1 50.0 1.0 C4C T:HEM201 3.1 50.0 1.0 C4B T:HEM201 3.1 50.0 1.0 CE T:MET52 3.4 50.0 1.0 CHA T:HEM201 3.4 50.0 1.0 CHC T:HEM201 3.4 50.0 1.0 CHB T:HEM201 3.4 50.0 1.0 CHD T:HEM201 3.5 50.0 1.0 CG T:MET52 3.5 50.0 1.0 CB T:MET52 3.9 50.0 1.0 CG S:MET52 3.9 50.0 1.0 CE S:MET52 4.0 50.0 1.0 C3A T:HEM201 4.3 50.0 1.0 C2A T:HEM201 4.3 50.0 1.0 C3D T:HEM201 4.3 50.0 1.0 C2B T:HEM201 4.3 50.0 1.0 C2D T:HEM201 4.3 50.0 1.0 C2C T:HEM201 4.3 50.0 1.0 C3C T:HEM201 4.3 50.0 1.0 C3B T:HEM201 4.3 50.0 1.0 CB S:MET52 4.7 50.0 1.0 CD1 T:ILE49 4.8 50.0 1.0

R.A.Warmack, R.A.Warmack. N/A N/A.