Zinc in PDB 6p8l: Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)

All present enzymatic activity of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data):
1.16.3.1;

The structure of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data), PDB code: 6p8l was solved by A.B.Taylor, D.Cioloboc, D.M.Kurtz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	92.65 / 2.10
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	207.918, 207.918, 143.046, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 24

The structure of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) also contains other interesting chemical elements:

Sodium

(Na)

4 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Zinc atom in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) (pdb code 6p8l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 24 binding sites of Zinc where determined in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data), PDB code: 6p8l:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:55.0 occ:0.36 OE1 A:GLU18 2.0 43.2 1.0 ND1 A:HIS54 2.2 28.4 1.0 OE2 A:GLU127 2.3 51.7 1.0 OE1 A:GLU51 2.4 46.1 1.0 OE2 A:GLU51 2.6 46.3 1.0 CD A:GLU51 2.6 38.9 1.0 CD A:GLU18 2.6 34.0 1.0 OE2 A:GLU18 2.6 37.6 1.0 CG A:HIS54 3.1 28.8 1.0 CE1 A:HIS54 3.2 30.7 1.0 CD A:GLU127 3.3 40.8 1.0 CB A:HIS54 3.4 25.3 1.0 CA A:GLU51 3.6 28.2 1.0 OE1 A:GLU127 3.6 46.0 1.0 CG A:GLU51 3.7 33.2 1.0 CB A:GLU51 3.8 26.8 1.0 CG A:GLU18 4.1 39.4 1.0 NE2 A:HIS54 4.3 31.2 1.0 CD2 A:HIS54 4.3 22.2 1.0 N A:GLU51 4.3 26.2 1.0 O A:ASP50 4.4 30.2 1.0 O A:GLU51 4.5 28.7 1.0 CG2 A:ILE123 4.5 27.3 1.0 C A:GLU51 4.5 31.0 1.0 C A:ASP50 4.6 32.2 1.0 CG A:GLU127 4.6 37.3 1.0 CB A:GLU18 4.7 29.5 1.0 CA A:HIS54 4.8 24.9 1.0 O A:HOH334 5.0 44.7 1.0 O A:HOH306 5.0 31.9 1.0

Zinc binding site 2 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:43.5 occ:0.18 ZN B:ZNH201 0.0 43.5 0.2 ZN B:ZNH201 0.1 43.8 0.2 NC B:ZNH201 2.1 39.8 0.3 ND B:ZNH201 2.1 42.9 0.3 NC B:ZNH201 2.2 39.1 0.3 NA B:ZNH201 2.2 42.9 0.3 ND B:ZNH201 2.2 41.3 0.3 NB B:ZNH201 2.2 40.2 0.3 SD B:MET52 2.2 36.9 1.0 NB B:ZNH201 2.3 39.3 0.3 NA B:ZNH201 2.3 41.3 0.3 SD A:MET52 2.4 37.9 1.0 CE B:MET52 3.0 33.6 1.0 C1D B:ZNH201 3.1 41.2 0.3 C4C B:ZNH201 3.1 40.3 0.3 C1C B:ZNH201 3.1 35.6 0.3 C4D B:ZNH201 3.1 43.9 0.3 C1C B:ZNH201 3.1 33.4 0.3 C4A B:ZNH201 3.2 41.3 0.3 C1D B:ZNH201 3.2 40.7 0.3 C4C B:ZNH201 3.2 37.5 0.3 C1A B:ZNH201 3.2 43.9 0.3 C4D B:ZNH201 3.2 42.3 0.3 C4B B:ZNH201 3.2 36.1 0.3 C1B B:ZNH201 3.2 40.0 0.3 C4B B:ZNH201 3.2 33.8 0.3 C1A B:ZNH201 3.2 42.3 0.3 CE A:MET52 3.3 34.0 1.0 C4A B:ZNH201 3.3 40.7 0.3 C1B B:ZNH201 3.3 37.2 0.3 CHD B:ZNH201 3.4 38.5 0.3 CG B:MET52 3.5 32.7 1.0 CHC B:ZNH201 3.5 33.5 0.3 CHC B:ZNH201 3.5 33.2 0.3 CHD B:ZNH201 3.5 38.2 0.3 CHB B:ZNH201 3.5 38.8 0.3 CHA B:ZNH201 3.5 44.3 0.3 CHA B:ZNH201 3.6 44.3 0.3 CG A:MET52 3.6 33.6 1.0 CHB B:ZNH201 3.7 38.3 0.3 CB B:MET52 4.3 28.0 1.0 CB A:MET52 4.3 34.6 1.0 C3C B:ZNH201 4.4 34.3 0.3 C2D B:ZNH201 4.4 39.2 0.3 C2C B:ZNH201 4.4 33.8 0.3 C3D B:ZNH201 4.4 42.6 0.3 C3C B:ZNH201 4.4 31.2 0.3 C2A B:ZNH201 4.5 42.6 0.3 C2C B:ZNH201 4.5 29.1 0.3 C3A B:ZNH201 4.5 39.3 0.3 C2D B:ZNH201 4.5 40.1 0.3 C3D B:ZNH201 4.5 41.2 0.3 C3B B:ZNH201 4.5 33.2 0.3 C2B B:ZNH201 4.5 33.8 0.3 C3B B:ZNH201 4.5 28.9 0.3 C2A B:ZNH201 4.6 41.3 0.3 C3A B:ZNH201 4.6 40.1 0.3 C2B B:ZNH201 4.6 30.4 0.3 CD1 B:ILE49 5.0 37.9 1.0

Zinc binding site 3 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:43.8 occ:0.18 ZN B:ZNH201 0.0 43.8 0.2 ZN B:ZNH201 0.1 43.5 0.2 ND B:ZNH201 2.1 41.3 0.3 NC B:ZNH201 2.1 39.1 0.3 NA B:ZNH201 2.2 41.3 0.3 ND B:ZNH201 2.2 42.9 0.3 NB B:ZNH201 2.2 39.3 0.3 NC B:ZNH201 2.2 39.8 0.3 SD B:MET52 2.2 36.9 1.0 NA B:ZNH201 2.3 42.9 0.3 NB B:ZNH201 2.3 40.2 0.3 SD A:MET52 2.4 37.9 1.0 CE B:MET52 3.0 33.6 1.0 C1D B:ZNH201 3.0 40.7 0.3 C4C B:ZNH201 3.0 37.5 0.3 C4D B:ZNH201 3.1 42.3 0.3 C1C B:ZNH201 3.1 33.4 0.3 C1C B:ZNH201 3.1 35.6 0.3 C4D B:ZNH201 3.2 43.9 0.3 C4A B:ZNH201 3.2 40.7 0.3 C4B B:ZNH201 3.2 33.8 0.3 C1D B:ZNH201 3.2 41.2 0.3 C1A B:ZNH201 3.2 42.3 0.3 C1B B:ZNH201 3.2 37.2 0.3 C4C B:ZNH201 3.2 40.3 0.3 C1A B:ZNH201 3.2 43.9 0.3 C4B B:ZNH201 3.3 36.1 0.3 C4A B:ZNH201 3.3 41.3 0.3 C1B B:ZNH201 3.3 40.0 0.3 CE A:MET52 3.3 34.0 1.0 CHD B:ZNH201 3.4 38.2 0.3 CHC B:ZNH201 3.5 33.5 0.3 CHB B:ZNH201 3.5 38.3 0.3 CHA B:ZNH201 3.5 44.3 0.3 CHD B:ZNH201 3.5 38.5 0.3 CHA B:ZNH201 3.5 44.3 0.3 CG B:MET52 3.5 32.7 1.0 CHC B:ZNH201 3.5 33.2 0.3 CG A:MET52 3.5 33.6 1.0 CHB B:ZNH201 3.7 38.8 0.3 CB A:MET52 4.2 34.6 1.0 C2D B:ZNH201 4.3 40.1 0.3 C3C B:ZNH201 4.3 31.2 0.3 C3D B:ZNH201 4.4 41.2 0.3 CB B:MET52 4.4 28.0 1.0 C2C B:ZNH201 4.4 29.1 0.3 C3B B:ZNH201 4.5 28.9 0.3 C3D B:ZNH201 4.5 42.6 0.3 C3A B:ZNH201 4.5 40.1 0.3 C2A B:ZNH201 4.5 41.3 0.3 C3C B:ZNH201 4.5 34.3 0.3 C2D B:ZNH201 4.5 39.2 0.3 C2C B:ZNH201 4.5 33.8 0.3 C2B B:ZNH201 4.5 30.4 0.3 C2A B:ZNH201 4.5 42.6 0.3 C3A B:ZNH201 4.6 39.3 0.3 C3B B:ZNH201 4.6 33.2 0.3 C2B B:ZNH201 4.6 33.8 0.3 CD1 B:ILE49 4.9 37.9 1.0

Zinc binding site 4 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:65.7 occ:0.35 OE1 B:GLU18 2.0 37.6 1.0 OE2 B:GLU127 2.2 52.6 1.0 OE2 B:GLU51 2.3 43.7 1.0 OE2 B:GLU18 2.3 36.1 1.0 CD B:GLU18 2.5 35.7 1.0 ND1 B:HIS54 2.5 25.8 1.0 OE1 B:GLU51 2.5 47.6 1.0 CD B:GLU51 2.5 41.8 1.0 CD B:GLU127 2.9 41.9 1.0 OE1 B:GLU127 3.1 46.1 1.0 CE1 B:HIS54 3.3 26.4 1.0 CG B:HIS54 3.6 30.6 1.0 CG B:GLU51 3.8 31.1 1.0 CB B:HIS54 3.9 29.0 1.0 CA B:GLU51 4.0 25.0 1.0 CG B:GLU18 4.0 26.1 1.0 CB B:GLU51 4.1 26.6 1.0 O B:HOH380 4.2 45.9 1.0 CG B:GLU127 4.2 27.2 1.0 CG2 B:ILE123 4.5 28.7 1.0 NE2 B:HIS54 4.5 32.6 1.0 CD2 B:HIS54 4.7 25.3 1.0 N B:GLU51 4.7 25.3 1.0 CB B:GLU18 4.7 23.1 1.0 O B:HOH312 4.9 24.2 1.0

Zinc binding site 5 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:57.1 occ:0.33 OE2 C:GLU127 2.1 51.2 1.0 OE1 C:GLU18 2.2 42.4 1.0 OE1 C:GLU51 2.2 50.6 1.0 OE2 C:GLU51 2.3 45.6 1.0 ND1 C:HIS54 2.3 30.0 1.0 CD C:GLU51 2.4 39.3 1.0 OE2 C:GLU18 2.6 44.6 1.0 CD C:GLU18 2.7 37.5 1.0 CD C:GLU127 3.0 41.5 1.0 OE1 C:GLU127 3.2 45.3 1.0 CE1 C:HIS54 3.2 29.2 1.0 CG C:HIS54 3.3 33.6 1.0 CG C:GLU51 3.6 35.5 1.0 CB C:HIS54 3.7 23.9 1.0 CA C:GLU51 3.7 28.4 1.0 CB C:GLU51 3.8 31.9 1.0 CG C:GLU18 4.2 34.1 1.0 CG C:GLU127 4.3 32.8 1.0 NE2 C:HIS54 4.3 28.9 1.0 CD2 C:HIS54 4.4 27.7 1.0 N C:GLU51 4.4 25.9 1.0 CG2 C:ILE123 4.6 23.5 1.0 O C:ASP50 4.6 31.9 1.0 O C:GLU51 4.7 33.3 1.0 C C:GLU51 4.8 30.1 1.0 C C:ASP50 4.8 31.9 1.0 CB C:GLU18 4.9 31.1 1.0 CE1 C:HIS130 4.9 49.3 1.0

Zinc binding site 6 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:42.1 occ:0.18 ZN D:ZNH201 0.0 42.1 0.2 ZN D:ZNH201 0.2 42.3 0.2 ND D:ZNH201 2.0 41.5 0.3 NC D:ZNH201 2.1 37.9 0.3 ND D:ZNH201 2.2 41.9 0.3 NA D:ZNH201 2.2 41.6 0.3 NB D:ZNH201 2.2 38.3 0.3 NC D:ZNH201 2.2 40.4 0.3 NA D:ZNH201 2.3 41.9 0.3 SD D:MET52 2.3 35.1 1.0 SD C:MET52 2.3 40.9 1.0 NB D:ZNH201 2.4 40.5 0.3 C1D D:ZNH201 2.9 39.3 0.3 C4C D:ZNH201 3.0 38.6 0.3 C4D D:ZNH201 3.0 41.7 0.3 C1C D:ZNH201 3.1 34.9 0.3 C4D D:ZNH201 3.2 40.9 0.3 CE D:MET52 3.2 35.4 1.0 C1A D:ZNH201 3.2 41.6 0.3 C4A D:ZNH201 3.2 39.5 0.3 C1D D:ZNH201 3.2 40.6 0.3 C1C D:ZNH201 3.2 35.2 0.3 C4C D:ZNH201 3.2 38.5 0.3 C4B D:ZNH201 3.2 35.5 0.3 C1B D:ZNH201 3.2 38.7 0.3 C1A D:ZNH201 3.2 40.9 0.3 CE C:MET52 3.3 37.4 1.0 CHD D:ZNH201 3.3 39.1 0.3 C4B D:ZNH201 3.3 35.2 0.3 C4A D:ZNH201 3.3 40.5 0.3 C1B D:ZNH201 3.4 38.4 0.3 CHA D:ZNH201 3.5 41.0 0.3 CHC D:ZNH201 3.5 35.2 0.3 CHB D:ZNH201 3.5 39.3 0.3 CHD D:ZNH201 3.5 40.3 0.3 CHA D:ZNH201 3.5 40.8 0.3 CG C:MET52 3.5 37.2 1.0 CG D:MET52 3.5 32.4 1.0 CHC D:ZNH201 3.6 35.6 0.3 CHB D:ZNH201 3.8 40.6 0.3 C2D D:ZNH201 4.3 37.5 0.3 C3D D:ZNH201 4.3 39.8 0.3 C3C D:ZNH201 4.3 32.5 0.3 CB D:MET52 4.3 30.0 1.0 CB C:MET52 4.3 28.1 1.0 C2C D:ZNH201 4.4 30.3 0.3 C3C D:ZNH201 4.4 32.6 0.3 C3D D:ZNH201 4.5 39.2 0.3 C2A D:ZNH201 4.5 39.9 0.3 C2D D:ZNH201 4.5 36.9 0.3 C3B D:ZNH201 4.5 29.6 0.3 C3A D:ZNH201 4.5 37.3 0.3 C2C D:ZNH201 4.5 33.8 0.3 C2B D:ZNH201 4.5 32.6 0.3 C2A D:ZNH201 4.6 39.2 0.3 C3A D:ZNH201 4.6 36.7 0.3 C3B D:ZNH201 4.6 32.3 0.3 C2B D:ZNH201 4.7 33.0 0.3

Zinc binding site 7 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:42.3 occ:0.18 ZN D:ZNH201 0.0 42.3 0.2 ZN D:ZNH201 0.2 42.1 0.2 NC D:ZNH201 2.0 40.4 0.3 ND D:ZNH201 2.0 41.9 0.3 NA D:ZNH201 2.2 41.9 0.3 NC D:ZNH201 2.2 37.9 0.3 ND D:ZNH201 2.2 41.5 0.3 NB D:ZNH201 2.2 40.5 0.3 SD C:MET52 2.3 40.9 1.0 NB D:ZNH201 2.3 38.3 0.3 NA D:ZNH201 2.4 41.6 0.3 SD D:MET52 2.4 35.1 1.0 C4C D:ZNH201 2.9 38.5 0.3 C1D D:ZNH201 3.0 40.6 0.3 C1C D:ZNH201 3.0 35.2 0.3 CE D:MET52 3.1 35.4 1.0 C4D D:ZNH201 3.1 40.9 0.3 C4D D:ZNH201 3.1 41.7 0.3 C1C D:ZNH201 3.1 34.9 0.3 C4A D:ZNH201 3.2 40.5 0.3 C1A D:ZNH201 3.2 40.9 0.3 C4C D:ZNH201 3.2 38.6 0.3 C1D D:ZNH201 3.2 39.3 0.3 C4B D:ZNH201 3.2 35.2 0.3 C1B D:ZNH201 3.2 38.4 0.3 C4B D:ZNH201 3.2 35.5 0.3 CHD D:ZNH201 3.3 40.3 0.3 C1A D:ZNH201 3.3 41.6 0.3 CE C:MET52 3.3 37.4 1.0 C1B D:ZNH201 3.4 38.7 0.3 C4A D:ZNH201 3.4 39.5 0.3 CG C:MET52 3.4 37.2 1.0 CHC D:ZNH201 3.5 35.2 0.3 CHC D:ZNH201 3.5 35.6 0.3 CHD D:ZNH201 3.5 39.1 0.3 CHA D:ZNH201 3.5 41.0 0.3 CHB D:ZNH201 3.5 40.6 0.3 CHA D:ZNH201 3.6 40.8 0.3 CG D:MET52 3.6 32.4 1.0 CHB D:ZNH201 3.8 39.3 0.3 CB C:MET52 4.2 28.1 1.0 C3C D:ZNH201 4.2 32.6 0.3 C2D D:ZNH201 4.3 36.9 0.3 C2C D:ZNH201 4.3 33.8 0.3 C3D D:ZNH201 4.4 39.2 0.3 C3C D:ZNH201 4.5 32.5 0.3 C3D D:ZNH201 4.5 39.8 0.3 C2A D:ZNH201 4.5 39.2 0.3 C3A D:ZNH201 4.5 36.7 0.3 CB D:MET52 4.5 30.0 1.0 C3B D:ZNH201 4.5 32.3 0.3 C2C D:ZNH201 4.5 30.3 0.3 C2D D:ZNH201 4.5 37.5 0.3 C2B D:ZNH201 4.5 33.0 0.3 C3B D:ZNH201 4.6 29.6 0.3 C2A D:ZNH201 4.6 39.9 0.3 C2B D:ZNH201 4.7 32.6 0.3 C3A D:ZNH201 4.7 37.3 0.3

Zinc binding site 8 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn202 b:51.1 occ:0.34 OE1 D:GLU18 1.8 50.3 1.0 OE2 D:GLU51 2.0 42.1 1.0 CD D:GLU51 2.0 39.9 1.0 OE1 D:GLU51 2.2 49.0 1.0 ND1 D:HIS54 2.5 29.4 1.0 CD D:GLU18 2.6 31.6 1.0 OE2 D:GLU18 2.7 38.9 1.0 OE2 D:GLU127 2.8 52.3 1.0 CG D:GLU51 3.1 32.1 1.0 CA D:GLU51 3.2 27.7 1.0 CB D:GLU51 3.2 28.1 1.0 CE1 D:HIS54 3.5 31.2 1.0 CG D:HIS54 3.5 29.1 1.0 CD D:GLU127 3.5 40.1 1.0 OE1 D:GLU127 3.6 45.5 1.0 CB D:HIS54 3.7 27.6 1.0 N D:GLU51 4.0 27.4 1.0 CG D:GLU18 4.0 29.2 1.0 C D:GLU51 4.3 29.1 1.0 O D:GLU51 4.3 28.2 1.0 CB D:GLU18 4.5 25.4 1.0 O D:ASP50 4.5 33.2 1.0 C D:ASP50 4.6 36.2 1.0 NE2 D:HIS54 4.6 27.9 1.0 CD2 D:HIS54 4.6 26.5 1.0 O D:HOH381 4.6 41.9 1.0 CA D:GLU18 4.9 28.0 1.0 CG D:GLU127 5.0 27.9 1.0

Zinc binding site 9 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn201 b:49.4 occ:0.33 OE1 E:GLU51 1.9 46.5 1.0 OE1 E:GLU18 2.1 37.6 1.0 ND1 E:HIS54 2.2 29.7 1.0 CD E:GLU51 2.3 41.0 1.0 OE2 E:GLU127 2.4 57.1 1.0 OE2 E:GLU51 2.6 61.1 1.0 OE2 E:GLU18 2.7 31.2 1.0 CD E:GLU18 2.7 36.8 1.0 CE1 E:HIS54 3.1 27.9 1.0 CD E:GLU127 3.3 44.0 1.0 CG E:HIS54 3.3 31.0 1.0 OE1 E:GLU127 3.4 45.2 1.0 CA E:GLU51 3.5 27.4 1.0 CG E:GLU51 3.5 33.0 1.0 CB E:GLU51 3.7 27.4 1.0 CB E:HIS54 3.7 30.2 1.0 CG E:GLU18 4.1 31.8 1.0 N E:GLU51 4.1 26.8 1.0 NE2 E:HIS54 4.2 31.1 1.0 CD2 E:HIS54 4.4 26.7 1.0 O E:HOH406 4.4 48.1 1.0 O E:ASP50 4.4 30.8 1.0 C E:GLU51 4.5 30.0 1.0 O E:GLU51 4.6 28.8 1.0 C E:ASP50 4.6 30.0 1.0 CG E:GLU127 4.6 33.5 1.0 CG2 E:ILE123 4.8 28.6 1.0 CB E:GLU18 4.8 27.6 1.0 CE1 E:HIS130 4.8 45.5 1.0

Zinc binding site 10 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX (Zn Absorption Edge X-Ray Data) within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:44.9 occ:0.17 ZN F:ZNH201 0.0 44.9 0.2 ZN F:ZNH201 0.1 44.9 0.2 ND F:ZNH201 2.1 42.5 0.3 NC F:ZNH201 2.1 41.4 0.3 NC F:ZNH201 2.2 39.7 0.3 NA F:ZNH201 2.2 42.5 0.3 ND F:ZNH201 2.2 41.1 0.3 NB F:ZNH201 2.2 41.5 0.3 NB F:ZNH201 2.3 39.9 0.3 NA F:ZNH201 2.3 41.2 0.3 SD F:MET52 2.3 40.2 1.0 SD E:MET52 2.4 45.2 1.0 C1D F:ZNH201 3.1 42.9 0.3 C4C F:ZNH201 3.1 37.9 0.3 C1C F:ZNH201 3.1 36.2 0.3 C4D F:ZNH201 3.1 43.7 0.3 CE F:MET52 3.1 35.2 1.0 C1C F:ZNH201 3.1 35.9 0.3 C4D F:ZNH201 3.1 42.3 0.3 C1A F:ZNH201 3.2 43.7 0.3 C4B F:ZNH201 3.2 36.2 0.3 C4A F:ZNH201 3.2 42.7 0.3 C4C F:ZNH201 3.2 39.3 0.3 C1D F:ZNH201 3.2 40.1 0.3 C1B F:ZNH201 3.2 37.8 0.3 C4B F:ZNH201 3.2 36.5 0.3 C1A F:ZNH201 3.2 42.2 0.3 C4A F:ZNH201 3.3 40.3 0.3 CE E:MET52 3.3 41.6 1.0 C1B F:ZNH201 3.3 39.5 0.3 CG E:MET52 3.4 34.9 1.0 CG F:MET52 3.4 34.8 1.0 CHD F:ZNH201 3.4 40.3 0.3 CHC F:ZNH201 3.5 36.9 0.3 CHC F:ZNH201 3.5 37.3 0.3 CHA F:ZNH201 3.5 42.4 0.3 CHA F:ZNH201 3.5 42.3 0.3 CHB F:ZNH201 3.5 40.7 0.3 CHD F:ZNH201 3.5 39.6 0.3 CHB F:ZNH201 3.7 39.6 0.3 CB F:MET52 4.3 34.8 1.0 CB E:MET52 4.3 34.1 1.0 C3C F:ZNH201 4.4 32.8 0.3 C2D F:ZNH201 4.4 40.9 0.3 C3D F:ZNH201 4.4 42.0 0.3 C2C F:ZNH201 4.4 32.8 0.3 C3C F:ZNH201 4.5 34.6 0.3 C3D F:ZNH201 4.5 41.2 0.3 C2C F:ZNH201 4.5 33.6 0.3 C3B F:ZNH201 4.5 32.4 0.3 C2A F:ZNH201 4.5 42.2 0.3 C2D F:ZNH201 4.5 39.1 0.3 C3A F:ZNH201 4.5 40.7 0.3 C2B F:ZNH201 4.5 32.7 0.3 C3B F:ZNH201 4.5 33.6 0.3 C2A F:ZNH201 4.5 41.1 0.3 C3A F:ZNH201 4.6 39.4 0.3 C2B F:ZNH201 4.6 34.0 0.3

B.S.Benavides, S.Valandro, D.Cioloboc, A.B.Taylor, K.S.Schanze, D.M.Kurtz Jr.. Structure of A Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry V. 59 1618 2020.
ISSN: ISSN 0006-2960
PubMed: 32283930
DOI: 10.1021/ACS.BIOCHEM.9B01103