Iron in PDB 9h1u: Cryo-Em Structure of Heterooligomeric Bacterioferritin

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>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Iron atom in the Cryo-Em Structure of Heterooligomeric Bacterioferritin (pdb code 9h1u). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the Cryo-Em Structure of Heterooligomeric Bacterioferritin, PDB code: 9h1u:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:42.5 occ:1.00 FE B:HEM201 0.0 42.5 1.0 SD A:MET52 1.9 43.2 1.0 NC B:HEM201 2.1 31.5 1.0 NB B:HEM201 2.1 28.5 1.0 ND B:HEM201 2.1 31.0 1.0 NA B:HEM201 2.1 33.4 1.0 CE B:MET52 3.0 29.2 1.0 C1C B:HEM201 3.1 31.8 1.0 C4D B:HEM201 3.1 26.1 1.0 C4B B:HEM201 3.1 23.3 1.0 C1B B:HEM201 3.1 27.8 1.0 C1A B:HEM201 3.1 32.5 1.0 C4A B:HEM201 3.1 27.0 1.0 C4C B:HEM201 3.1 23.3 1.0 C1D B:HEM201 3.1 31.6 1.0 SD B:MET52 3.2 41.1 1.0 CG A:MET52 3.3 33.9 1.0 CE A:MET52 3.4 36.6 1.0 CHC B:HEM201 3.4 23.8 1.0 CHA B:HEM201 3.4 26.6 1.0 CHB B:HEM201 3.4 26.8 1.0 CHD B:HEM201 3.5 24.0 1.0 CB A:MET52 3.7 27.6 1.0 C2B B:HEM201 4.3 32.5 1.0 C2C B:HEM201 4.3 32.9 1.0 C3D B:HEM201 4.3 26.2 1.0 C3B B:HEM201 4.3 31.9 1.0 C3A B:HEM201 4.3 31.1 1.0 C2D B:HEM201 4.3 31.8 1.0 C3C B:HEM201 4.3 28.9 1.0 C2A B:HEM201 4.3 30.5 1.0 CG B:MET52 4.5 34.6 1.0 CB B:MET52 4.6 35.2 1.0

Iron binding site 2 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:64.0 occ:1.00 FE C:HEM201 0.0 64.0 1.0 SD C:MET52 2.0 53.7 1.0 NA C:HEM201 2.1 49.4 1.0 ND C:HEM201 2.1 45.5 1.0 NC C:HEM201 2.1 43.9 1.0 NB C:HEM201 2.1 41.7 1.0 CE C:MET52 2.7 32.2 1.0 CG C:MET52 2.8 36.5 1.0 SD D:MET52 2.9 54.7 1.0 C1A C:HEM201 3.0 44.3 1.0 C4D C:HEM201 3.0 45.7 1.0 C1C C:HEM201 3.1 39.2 1.0 C4B C:HEM201 3.1 37.8 1.0 C4A C:HEM201 3.1 43.0 1.0 C1D C:HEM201 3.1 43.9 1.0 C1B C:HEM201 3.1 43.7 1.0 C4C C:HEM201 3.1 47.5 1.0 CHA C:HEM201 3.4 40.9 1.0 CHC C:HEM201 3.4 38.4 1.0 CHB C:HEM201 3.5 45.0 1.0 CHD C:HEM201 3.5 43.8 1.0 CE D:MET52 3.5 38.8 1.0 CB C:MET52 3.9 27.8 1.0 CG D:MET52 4.0 44.6 1.0 C2A C:HEM201 4.3 41.5 1.0 C3D C:HEM201 4.3 45.1 1.0 C3A C:HEM201 4.3 41.6 1.0 C2C C:HEM201 4.3 41.9 1.0 C2D C:HEM201 4.3 44.8 1.0 C3B C:HEM201 4.3 43.3 1.0 C2B C:HEM201 4.3 44.2 1.0 C3C C:HEM201 4.3 42.3 1.0 CB D:MET52 4.5 35.1 1.0

Iron binding site 3 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:64.7 occ:1.00 FE E:HEM201 0.0 64.7 1.0 SD E:MET52 1.8 45.4 1.0 ND E:HEM201 2.0 40.7 1.0 NC E:HEM201 2.1 38.1 1.0 NA E:HEM201 2.1 41.2 1.0 NB E:HEM201 2.1 40.6 1.0 SD F:MET52 2.9 42.6 1.0 C4D E:HEM201 3.1 39.9 1.0 CE E:MET52 3.1 28.3 1.0 C1C E:HEM201 3.1 32.3 1.0 C1A E:HEM201 3.1 35.2 1.0 C1D E:HEM201 3.1 36.5 1.0 C4B E:HEM201 3.1 37.2 1.0 C4C E:HEM201 3.1 34.5 1.0 C4A E:HEM201 3.1 42.8 1.0 C1B E:HEM201 3.1 33.8 1.0 CG E:MET52 3.3 34.5 1.0 CHA E:HEM201 3.4 35.0 1.0 CHC E:HEM201 3.4 32.1 1.0 CHD E:HEM201 3.5 32.4 1.0 CHB E:HEM201 3.5 39.4 1.0 CG F:MET52 3.7 33.3 1.0 CE F:MET52 3.8 33.8 1.0 CB E:MET52 3.9 23.8 1.0 C3D E:HEM201 4.3 38.5 1.0 C2D E:HEM201 4.3 38.1 1.0 C2C E:HEM201 4.3 34.8 1.0 C2A E:HEM201 4.3 42.6 1.0 C3A E:HEM201 4.3 40.2 1.0 C3C E:HEM201 4.3 35.1 1.0 C3B E:HEM201 4.3 37.0 1.0 C2B E:HEM201 4.3 28.7 1.0 CB F:MET52 4.5 28.9 1.0 CD1 E:ILE49 5.0 36.5 1.0

Iron binding site 4 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe201 b:60.7 occ:1.00 FE G:HEM201 0.0 60.7 1.0 SD G:MET52 1.9 50.3 1.0 NC G:HEM201 2.0 46.6 1.0 ND G:HEM201 2.1 46.4 1.0 NA G:HEM201 2.1 46.0 1.0 NB G:HEM201 2.1 46.7 1.0 SD H:MET52 2.9 44.5 1.0 CE G:MET52 3.0 36.2 1.0 C1C G:HEM201 3.1 42.7 1.0 C1A G:HEM201 3.1 47.6 1.0 C4C G:HEM201 3.1 43.3 1.0 C4D G:HEM201 3.1 45.0 1.0 C1D G:HEM201 3.1 45.1 1.0 C4A G:HEM201 3.1 41.5 1.0 C4B G:HEM201 3.1 44.5 1.0 C1B G:HEM201 3.1 45.3 1.0 CHC G:HEM201 3.4 44.5 1.0 CHA G:HEM201 3.4 42.2 1.0 CHD G:HEM201 3.4 41.2 1.0 CHB G:HEM201 3.4 37.0 1.0 CG G:MET52 3.6 40.9 1.0 CE H:MET52 3.8 43.9 1.0 CG H:MET52 4.0 44.6 1.0 CB G:MET52 4.0 35.3 1.0 CB H:MET52 4.2 38.6 1.0 C2A G:HEM201 4.3 47.1 1.0 C3A G:HEM201 4.3 45.5 1.0 C2C G:HEM201 4.3 44.5 1.0 C2B G:HEM201 4.3 47.4 1.0 C3C G:HEM201 4.3 43.4 1.0 C2D G:HEM201 4.3 48.0 1.0 C3D G:HEM201 4.3 45.7 1.0 C3B G:HEM201 4.3 41.3 1.0 CD1 G:ILE49 4.9 35.3 1.0

Iron binding site 5 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe301 b:88.9 occ:1.00 OE1 M:GLU18 2.1 54.6 1.0 OE2 M:GLU51 2.2 54.7 1.0 CD M:GLU51 2.3 56.7 1.0 OE1 M:GLU51 2.4 56.2 1.0 ND1 M:HIS54 2.5 45.4 1.0 CD M:GLU18 2.8 52.1 1.0 OE2 M:GLU18 2.9 48.9 1.0 CE1 M:HIS54 3.4 43.7 1.0 CG M:GLU51 3.4 48.0 1.0 CG M:HIS54 3.5 49.6 1.0 CB M:HIS54 3.8 48.4 1.0 OG1 M:THR127 4.0 39.8 1.0 CA M:GLU51 4.3 49.8 1.0 CG M:GLU18 4.3 43.6 1.0 CE1 M:HIS131 4.3 49.1 1.0 CB M:GLU51 4.3 46.2 1.0 ND1 M:HIS131 4.5 49.9 1.0 NE2 M:HIS54 4.6 52.4 1.0 CD2 M:HIS54 4.6 49.9 1.0 CB M:GLU18 4.8 38.5 1.0 OE1 M:GLU94 4.9 46.0 1.0

Iron binding site 6 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe302 b:62.2 occ:1.00 OD1 A:ASN148 2.5 26.3 1.0 OE1 G:GLN151 2.6 29.4 1.0 OD1 G:ASN148 2.6 28.6 1.0 OD1 M:ASN149 2.7 30.7 1.0 OD1 U:ASN149 2.7 30.2 1.0 OE1 A:GLN151 2.9 34.0 1.0 OE1 U:GLN152 3.0 24.8 1.0 OE1 M:GLN152 3.1 22.8 1.0 CG A:ASN148 3.4 21.9 1.0 CG M:ASN149 3.5 21.8 1.0 CD G:GLN151 3.7 16.1 1.0 CG G:ASN148 3.7 27.6 1.0 ND2 M:ASN149 3.8 27.5 1.0 ND2 A:ASN148 3.8 25.5 1.0 CG U:ASN149 3.8 24.8 1.0 CD A:GLN151 3.8 23.0 1.0 CD U:GLN152 3.9 19.6 1.0 NE2 G:GLN151 4.1 14.6 1.0 CD M:GLN152 4.1 19.3 1.0 NE2 U:GLN152 4.1 29.5 1.0 NE2 A:GLN151 4.1 22.9 1.0 ND2 U:ASN149 4.4 17.2 1.0 NE2 M:GLN152 4.4 21.3 1.0 ND2 G:ASN148 4.4 26.7 1.0 CB A:ASN148 4.6 23.6 1.0 CB M:ASN149 4.8 18.9 1.0 CB G:ASN148 4.8 27.2 1.0 CA A:ASN148 4.9 19.5 1.0 CG G:GLN151 4.9 23.1 1.0 CB U:ASN149 5.0 19.0 1.0 CA G:ASN148 5.0 21.7 1.0

Iron binding site 7 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe301 b:90.3 occ:1.00 OE1 N:GLU51 2.2 52.7 1.0 OE1 N:GLU18 2.3 47.3 1.0 OE2 N:GLU51 2.3 58.7 1.0 CD N:GLU51 2.4 57.4 1.0 ND1 N:HIS54 2.5 49.2 1.0 CD N:GLU18 3.3 43.0 1.0 CE1 N:HIS54 3.4 51.0 1.0 CG N:HIS54 3.5 48.4 1.0 CG N:GLU51 3.7 48.6 1.0 CB N:HIS54 3.8 44.0 1.0 OE2 N:GLU18 3.9 39.7 1.0 CA N:GLU51 4.0 46.2 1.0 OG1 N:THR127 4.2 48.2 1.0 CB N:GLU51 4.2 47.0 1.0 CG N:GLU18 4.3 34.1 1.0 NE2 N:HIS54 4.6 51.9 1.0 CB N:GLU18 4.6 28.6 1.0 CD2 N:HIS54 4.7 44.8 1.0 NE2 N:HIS131 4.8 45.3 1.0 N N:GLU51 4.8 43.2 1.0 CE1 N:HIS131 4.8 45.9 1.0 O N:GLU51 4.9 52.9 1.0 O N:ASP50 5.0 48.9 1.0 CA N:GLU18 5.0 29.8 1.0 C N:GLU51 5.0 51.3 1.0

Iron binding site 8 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe302 b:60.2 occ:1.00 OE1 J:GLN152 2.6 30.8 1.0 OD1 D:ASN148 2.6 22.8 1.0 OD1 N:ASN149 2.8 27.7 1.0 OE1 S:GLN152 2.8 28.2 1.0 OD1 J:ASN149 2.9 31.8 1.0 OE1 N:GLN152 2.9 24.0 1.0 OE1 D:GLN151 3.0 21.2 1.0 OD1 S:ASN149 3.0 23.6 1.0 CD J:GLN152 3.6 20.0 1.0 CG J:ASN149 3.7 16.5 1.0 CG D:ASN148 3.7 18.9 1.0 CG S:ASN149 3.8 14.2 1.0 CD S:GLN152 3.8 23.3 1.0 NE2 J:GLN152 3.9 22.7 1.0 CD N:GLN152 3.9 19.3 1.0 CG N:ASN149 3.9 24.6 1.0 CD D:GLN151 4.0 22.5 1.0 ND2 J:ASN149 4.0 14.4 1.0 NE2 S:GLN152 4.1 24.4 1.0 ND2 S:ASN149 4.1 16.5 1.0 NE2 N:GLN152 4.2 23.0 1.0 ND2 D:ASN148 4.2 26.6 1.0 NE2 D:GLN151 4.4 24.1 1.0 ND2 N:ASN149 4.6 23.6 1.0 CB J:ASN149 4.8 16.2 1.0 CB S:ASN149 4.9 15.2 1.0 CB D:ASN148 4.9 17.6 1.0 CG J:GLN152 4.9 9.9 1.0

Iron binding site 9 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ O:Fe301 b:94.0 occ:1.00 OE1 O:GLU18 2.1 47.9 1.0 OE2 O:GLU51 2.1 59.8 1.0 CD O:GLU51 2.3 56.9 1.0 OE1 O:GLU51 2.5 56.6 1.0 ND1 O:HIS54 2.5 49.8 1.0 CD O:GLU18 3.0 50.2 1.0 OE2 O:GLU18 3.2 49.1 1.0 CG O:HIS54 3.4 46.9 1.0 CE1 O:HIS54 3.5 48.9 1.0 CG O:GLU51 3.5 48.5 1.0 CA O:GLU51 3.5 46.9 1.0 CB O:HIS54 3.5 41.2 1.0 CB O:GLU51 3.9 46.2 1.0 O O:GLU51 4.2 55.8 1.0 N O:GLU51 4.3 52.5 1.0 CG O:GLU18 4.4 43.1 1.0 C O:GLU51 4.4 51.5 1.0 O O:ASP50 4.4 50.1 1.0 CD2 O:HIS54 4.5 51.7 1.0 NE2 O:HIS54 4.6 51.1 1.0 OG1 O:THR127 4.7 46.5 1.0 C O:ASP50 4.7 53.2 1.0 CB O:GLU18 4.7 33.5 1.0 NE2 O:HIS131 4.9 55.6 1.0 CE1 O:HIS131 4.9 56.0 1.0 CA O:HIS54 5.0 41.6 1.0

Iron binding site 10 out of 20 in the Cryo-Em Structure of Heterooligomeric Bacterioferritin


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 Heterooligomeric Bacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ Q:Fe301 b:78.2 occ:1.00 OE1 Q:GLU18 2.5 45.2 1.0 OE2 Q:GLU18 2.7 47.3 1.0 ND1 Q:HIS54 2.7 45.9 1.0 OE2 Q:GLU51 2.9 52.3 1.0 CD Q:GLU18 2.9 45.2 1.0 OE1 Q:GLU51 3.3 53.0 1.0 CD Q:GLU51 3.4 52.3 1.0 OG1 Q:THR127 3.5 44.4 1.0 CE1 Q:HIS54 3.6 47.0 1.0 CG Q:HIS54 3.7 40.2 1.0 CB Q:HIS54 3.9 34.2 1.0 CG Q:GLU18 4.4 35.8 1.0 OE1 Q:GLU94 4.7 49.4 1.0 CB Q:THR127 4.7 41.4 1.0 NE2 Q:HIS54 4.8 48.9 1.0 CG Q:GLU51 4.8 41.5 1.0 CD2 Q:HIS54 4.8 47.6 1.0 CA Q:GLU51 4.8 42.1 1.0 O Q:LEU123 5.0 45.4 1.0

D.Stein, B.Jartoux, S.Dror, T.C.T.Koubkova-Yu, R.Zalk, A.Shahar, R.Uebe, R.Zarivach, A.G.Frank. The Negative Design Principles of Hetero-Oligomeric Ferritin Revealed By Cryo-Em and Graph-Theory Analysis To Be Published.