Zinc in PDB 6p8k: Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX

All present enzymatic activity of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX:
1.16.3.1;

The structure of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX, PDB code: 6p8k 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)	19.96 / 1.70
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	207.852, 207.852, 142.657, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 21.8

The structure of Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX 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 (pdb code 6p8k). 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, PDB code: 6p8k:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:36.7 occ:0.35 OE2 A:GLU51 2.0 32.2 1.0 ND1 A:HIS54 2.1 18.4 1.0 OE2 A:GLU127 2.2 38.7 1.0 OE1 A:GLU18 2.2 28.8 1.0 CD A:GLU51 2.4 31.6 1.0 OE1 A:GLU51 2.4 37.6 1.0 OE2 A:GLU18 2.7 28.9 1.0 CD A:GLU18 2.8 27.2 1.0 CE1 A:HIS54 2.9 19.2 1.0 CD A:GLU127 3.1 34.7 1.0 CG A:HIS54 3.2 16.9 1.0 OE1 A:GLU127 3.3 37.1 1.0 CG A:GLU51 3.6 24.9 1.0 CB A:HIS54 3.6 16.3 1.0 CA A:GLU51 3.7 18.0 1.0 CB A:GLU51 3.9 21.2 1.0 NE2 A:HIS54 4.1 19.1 1.0 CD2 A:HIS54 4.3 17.6 1.0 CG A:GLU18 4.3 22.9 1.0 N A:GLU51 4.4 15.8 1.0 CG A:GLU127 4.4 27.0 1.0 O A:HOH427 4.5 49.1 1.0 O A:ASP50 4.5 18.6 1.0 CG2 A:ILE123 4.6 17.3 1.0 O A:GLU51 4.7 18.7 1.0 C A:GLU51 4.7 18.6 1.0 C A:ASP50 4.7 18.0 1.0 CE1 A:HIS130 4.9 35.3 1.0 CB A:GLU18 5.0 19.6 1.0

Zinc binding site 2 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:32.9 occ:0.27 ZN A:ZNH202 0.0 32.9 0.3 ZN A:ZNH202 0.1 31.4 0.3 NC A:ZNH202 2.1 32.5 0.4 ND A:ZNH202 2.1 33.4 0.4 NC A:ZNH202 2.2 33.0 0.4 NA A:ZNH202 2.2 34.6 0.4 ND A:ZNH202 2.2 34.2 0.4 NB A:ZNH202 2.2 33.5 0.4 NB A:ZNH202 2.3 31.7 0.4 NA A:ZNH202 2.3 33.0 0.4 SD B:MET52 2.4 26.2 1.0 SD A:MET52 2.5 27.4 1.0 C1D A:ZNH202 3.1 33.6 0.4 C4C A:ZNH202 3.1 33.3 0.4 C1C A:ZNH202 3.1 32.0 0.4 CE A:MET52 3.1 27.7 1.0 C4D A:ZNH202 3.1 34.2 0.4 C1C A:ZNH202 3.1 32.2 0.4 C4A A:ZNH202 3.2 34.8 0.4 C1D A:ZNH202 3.2 34.5 0.4 C4C A:ZNH202 3.2 33.1 0.4 C1A A:ZNH202 3.2 35.2 0.4 C4D A:ZNH202 3.2 35.1 0.4 C4B A:ZNH202 3.2 32.7 0.4 C1B A:ZNH202 3.2 34.2 0.4 C4B A:ZNH202 3.2 30.8 0.4 CE B:MET52 3.2 27.7 1.0 C1A A:ZNH202 3.2 34.1 0.4 C4A A:ZNH202 3.3 33.5 0.4 C1B A:ZNH202 3.3 31.3 0.4 CHD A:ZNH202 3.4 33.8 0.4 CHC A:ZNH202 3.5 31.3 0.4 CHC A:ZNH202 3.5 31.9 0.4 CHD A:ZNH202 3.5 34.0 0.4 CHB A:ZNH202 3.5 35.0 0.4 CHA A:ZNH202 3.5 35.1 0.4 CHA A:ZNH202 3.6 34.2 0.4 CG B:MET52 3.6 22.0 1.0 CHB A:ZNH202 3.7 32.7 0.4 CG A:MET52 3.7 20.5 1.0 CB B:MET52 4.3 19.1 1.0 C3C A:ZNH202 4.4 32.4 0.4 C2D A:ZNH202 4.4 33.4 0.4 C2C A:ZNH202 4.4 32.4 0.4 C3D A:ZNH202 4.4 35.2 0.4 CB A:MET52 4.4 18.3 1.0 C3C A:ZNH202 4.4 32.4 0.4 C2A A:ZNH202 4.5 36.1 0.4 C2C A:ZNH202 4.5 31.9 0.4 C3A A:ZNH202 4.5 34.5 0.4 C2D A:ZNH202 4.5 35.2 0.4 C3D A:ZNH202 4.5 36.3 0.4 C3B A:ZNH202 4.5 32.5 0.4 C2B A:ZNH202 4.5 32.9 0.4 C3B A:ZNH202 4.5 29.2 0.4 C2A A:ZNH202 4.6 35.4 0.4 C3A A:ZNH202 4.6 34.2 0.4 C2B A:ZNH202 4.6 29.6 0.4

Zinc binding site 3 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:31.4 occ:0.27 ZN A:ZNH202 0.0 31.4 0.3 ZN A:ZNH202 0.1 32.9 0.3 ND A:ZNH202 2.1 34.2 0.4 NC A:ZNH202 2.1 33.0 0.4 ND A:ZNH202 2.2 33.4 0.4 NA A:ZNH202 2.2 33.0 0.4 NB A:ZNH202 2.2 31.7 0.4 NC A:ZNH202 2.2 32.5 0.4 NA A:ZNH202 2.3 34.6 0.4 NB A:ZNH202 2.3 33.5 0.4 SD B:MET52 2.4 26.2 1.0 SD A:MET52 2.4 27.4 1.0 C1D A:ZNH202 3.0 34.5 0.4 C4C A:ZNH202 3.0 33.1 0.4 C4D A:ZNH202 3.1 35.1 0.4 C1C A:ZNH202 3.1 32.2 0.4 CE A:MET52 3.1 27.7 1.0 C1C A:ZNH202 3.2 32.0 0.4 C4D A:ZNH202 3.2 34.2 0.4 C4A A:ZNH202 3.2 33.5 0.4 C4B A:ZNH202 3.2 30.8 0.4 CE B:MET52 3.2 27.7 1.0 C1D A:ZNH202 3.2 33.6 0.4 C1A A:ZNH202 3.2 34.1 0.4 C1B A:ZNH202 3.2 31.3 0.4 C4C A:ZNH202 3.2 33.3 0.4 C1A A:ZNH202 3.2 35.2 0.4 C4B A:ZNH202 3.3 32.7 0.4 C4A A:ZNH202 3.3 34.8 0.4 C1B A:ZNH202 3.3 34.2 0.4 CHD A:ZNH202 3.4 34.0 0.4 CHC A:ZNH202 3.5 31.3 0.4 CHB A:ZNH202 3.5 32.7 0.4 CHA A:ZNH202 3.5 35.1 0.4 CHD A:ZNH202 3.5 33.8 0.4 CHA A:ZNH202 3.5 34.2 0.4 CHC A:ZNH202 3.5 31.9 0.4 CG A:MET52 3.6 20.5 1.0 CG B:MET52 3.7 22.0 1.0 CHB A:ZNH202 3.7 35.0 0.4 CB A:MET52 4.3 18.3 1.0 C2D A:ZNH202 4.3 35.2 0.4 C3C A:ZNH202 4.3 32.4 0.4 C3D A:ZNH202 4.4 36.3 0.4 C2C A:ZNH202 4.4 31.9 0.4 CB B:MET52 4.4 19.1 1.0 C3B A:ZNH202 4.5 29.2 0.4 C3D A:ZNH202 4.5 35.2 0.4 C3A A:ZNH202 4.5 34.2 0.4 C2A A:ZNH202 4.5 35.4 0.4 C3C A:ZNH202 4.5 32.4 0.4 C2D A:ZNH202 4.5 33.4 0.4 C2C A:ZNH202 4.5 32.4 0.4 C2B A:ZNH202 4.5 29.6 0.4 C2A A:ZNH202 4.5 36.1 0.4 C3A A:ZNH202 4.6 34.5 0.4 C3B A:ZNH202 4.6 32.5 0.4 C2B A:ZNH202 4.6 32.9 0.4

Zinc binding site 4 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:44.0 occ:0.31 OE2 B:GLU51 1.8 30.8 1.0 ND1 B:HIS54 2.1 17.1 1.0 OE2 B:GLU127 2.1 39.6 1.0 OE1 B:GLU18 2.2 27.0 1.0 CD B:GLU51 2.4 28.8 1.0 OE2 B:GLU18 2.5 25.6 1.0 CD B:GLU18 2.7 23.6 1.0 OE1 B:GLU51 2.7 35.1 1.0 CD B:GLU127 2.9 33.9 1.0 CE1 B:HIS54 3.0 16.4 1.0 OE1 B:GLU127 3.1 35.9 1.0 CG B:HIS54 3.2 16.5 1.0 CB B:HIS54 3.7 16.5 1.0 CG B:GLU51 3.7 21.8 1.0 CA B:GLU51 3.8 17.4 1.0 CB B:GLU51 4.0 18.0 1.0 NE2 B:HIS54 4.1 17.2 1.0 CG B:GLU18 4.2 19.4 1.0 CD2 B:HIS54 4.3 17.3 1.0 CG B:GLU127 4.3 26.7 1.0 O B:HOH419 4.4 39.9 1.0 CG2 B:ILE123 4.5 14.6 1.0 N B:GLU51 4.6 16.7 1.0 O B:ASP50 4.7 19.0 1.0 O B:GLU51 4.8 20.2 1.0 C B:GLU51 4.9 18.6 1.0 CB B:GLU18 4.9 18.4 1.0 O B:HOH327 4.9 20.4 1.0 C B:ASP50 4.9 18.6 1.0

Zinc binding site 5 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:48.3 occ:0.35 OE2 C:GLU127 2.0 38.4 1.0 OE2 C:GLU51 2.1 32.0 1.0 OE1 C:GLU18 2.1 27.1 1.0 ND1 C:HIS54 2.1 14.8 1.0 OE2 C:GLU18 2.3 25.1 1.0 CD C:GLU18 2.5 24.3 1.0 CD C:GLU51 2.6 30.3 1.0 OE1 C:GLU51 2.7 37.0 1.0 CD C:GLU127 3.0 34.4 1.0 CE1 C:HIS54 3.0 15.2 1.0 CG C:HIS54 3.2 14.4 1.0 OE1 C:GLU127 3.3 37.5 1.0 CB C:HIS54 3.6 13.3 1.0 CG C:GLU51 3.9 23.7 1.0 CA C:GLU51 4.0 17.3 1.0 CG C:GLU18 4.0 21.1 1.0 CB C:GLU51 4.1 18.9 1.0 NE2 C:HIS54 4.2 16.6 1.0 CG C:GLU127 4.2 27.8 1.0 CD2 C:HIS54 4.3 13.6 1.0 CG2 C:ILE123 4.3 16.4 1.0 O C:HOH446 4.3 36.4 1.0 N C:GLU51 4.7 16.4 1.0 O C:HOH327 4.8 21.5 1.0 O C:ASP50 4.8 17.1 1.0 O C:GLU51 4.8 18.4 1.0 CB C:GLU18 4.8 19.0 1.0 C C:GLU51 4.9 17.6 1.0

Zinc binding site 6 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn202 b:31.1 occ:0.28 ZN C:ZNH202 0.0 31.1 0.3 ZN C:ZNH202 0.2 33.7 0.3 ND C:ZNH202 2.0 35.0 0.4 NC C:ZNH202 2.1 33.3 0.4 ND C:ZNH202 2.2 33.2 0.4 NA C:ZNH202 2.2 33.4 0.4 NB C:ZNH202 2.2 31.7 0.4 NC C:ZNH202 2.2 31.8 0.4 NA C:ZNH202 2.3 35.4 0.4 NB C:ZNH202 2.4 33.8 0.4 SD C:MET52 2.4 27.5 1.0 SD D:MET52 2.4 25.1 1.0 C1D C:ZNH202 2.9 34.9 0.4 C4C C:ZNH202 3.0 33.7 0.4 C4D C:ZNH202 3.0 35.5 0.4 C1C C:ZNH202 3.1 32.4 0.4 CE D:MET52 3.1 25.9 1.0 C4D C:ZNH202 3.2 34.3 0.4 C1A C:ZNH202 3.2 34.2 0.4 C4A C:ZNH202 3.2 33.8 0.4 C1D C:ZNH202 3.2 33.7 0.4 C1C C:ZNH202 3.2 31.5 0.4 C4C C:ZNH202 3.2 32.6 0.4 C4B C:ZNH202 3.2 31.2 0.4 C1B C:ZNH202 3.2 32.2 0.4 CE C:MET52 3.2 27.8 1.0 C1A C:ZNH202 3.2 36.2 0.4 CHD C:ZNH202 3.3 34.5 0.4 C4B C:ZNH202 3.3 33.0 0.4 C4A C:ZNH202 3.3 35.7 0.4 C1B C:ZNH202 3.4 34.2 0.4 CHA C:ZNH202 3.5 35.8 0.4 CHB C:ZNH202 3.5 33.2 0.4 CHC C:ZNH202 3.5 31.3 0.4 CHD C:ZNH202 3.5 33.5 0.4 CHA C:ZNH202 3.5 34.0 0.4 CHC C:ZNH202 3.6 32.6 0.4 CG C:MET52 3.6 21.2 1.0 CG D:MET52 3.6 20.4 1.0 CHB C:ZNH202 3.8 35.5 0.4 C2D C:ZNH202 4.3 35.1 0.4 C3D C:ZNH202 4.3 35.9 0.4 C3C C:ZNH202 4.3 32.2 0.4 CB D:MET52 4.3 19.0 1.0 C2C C:ZNH202 4.4 31.8 0.4 CB C:MET52 4.4 19.0 1.0 C3C C:ZNH202 4.4 31.6 0.4 C3D C:ZNH202 4.5 35.8 0.4 C2A C:ZNH202 4.5 35.4 0.4 C3B C:ZNH202 4.5 30.7 0.4 C2D C:ZNH202 4.5 34.4 0.4 C3A C:ZNH202 4.5 34.5 0.4 C2C C:ZNH202 4.5 31.3 0.4 C2B C:ZNH202 4.5 30.9 0.4 C2A C:ZNH202 4.6 37.5 0.4 C3A C:ZNH202 4.6 36.3 0.4 C3B C:ZNH202 4.6 33.3 0.4 C2B C:ZNH202 4.7 32.9 0.4

Zinc binding site 7 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn202 b:33.7 occ:0.28 ZN C:ZNH202 0.0 33.7 0.3 ZN C:ZNH202 0.2 31.1 0.3 NC C:ZNH202 2.0 31.8 0.4 ND C:ZNH202 2.0 33.2 0.4 NA C:ZNH202 2.2 35.4 0.4 NC C:ZNH202 2.2 33.3 0.4 ND C:ZNH202 2.2 35.0 0.4 NB C:ZNH202 2.2 33.8 0.4 NB C:ZNH202 2.3 31.7 0.4 NA C:ZNH202 2.4 33.4 0.4 SD C:MET52 2.4 27.5 1.0 SD D:MET52 2.5 25.1 1.0 C4C C:ZNH202 2.9 32.6 0.4 C1D C:ZNH202 3.0 33.7 0.4 C1C C:ZNH202 3.0 31.5 0.4 CE D:MET52 3.0 25.9 1.0 C4D C:ZNH202 3.1 34.3 0.4 C4D C:ZNH202 3.1 35.5 0.4 C1C C:ZNH202 3.1 32.4 0.4 C4A C:ZNH202 3.2 35.7 0.4 C1A C:ZNH202 3.2 36.2 0.4 C4C C:ZNH202 3.2 33.7 0.4 C1D C:ZNH202 3.2 34.9 0.4 C4B C:ZNH202 3.2 33.0 0.4 C1B C:ZNH202 3.2 34.2 0.4 C4B C:ZNH202 3.2 31.2 0.4 CE C:MET52 3.3 27.8 1.0 CHD C:ZNH202 3.3 33.5 0.4 C1A C:ZNH202 3.3 34.2 0.4 C1B C:ZNH202 3.4 32.2 0.4 C4A C:ZNH202 3.4 33.8 0.4 CHC C:ZNH202 3.5 31.3 0.4 CG C:MET52 3.5 21.2 1.0 CHC C:ZNH202 3.5 32.6 0.4 CHD C:ZNH202 3.5 34.5 0.4 CHA C:ZNH202 3.5 35.8 0.4 CHB C:ZNH202 3.5 35.5 0.4 CHA C:ZNH202 3.6 34.0 0.4 CG D:MET52 3.7 20.4 1.0 CHB C:ZNH202 3.8 33.2 0.4 C3C C:ZNH202 4.2 31.6 0.4 CB C:MET52 4.3 19.0 1.0 C2D C:ZNH202 4.3 34.4 0.4 C2C C:ZNH202 4.3 31.3 0.4 C3D C:ZNH202 4.4 35.8 0.4 C3C C:ZNH202 4.5 32.2 0.4 C3D C:ZNH202 4.5 35.9 0.4 C2A C:ZNH202 4.5 37.5 0.4 C3A C:ZNH202 4.5 36.3 0.4 C3B C:ZNH202 4.5 33.3 0.4 C2C C:ZNH202 4.5 31.8 0.4 CB D:MET52 4.5 19.0 1.0 C2D C:ZNH202 4.5 35.1 0.4 C2B C:ZNH202 4.5 32.9 0.4 C3B C:ZNH202 4.6 30.7 0.4 C2A C:ZNH202 4.6 35.4 0.4 C2B C:ZNH202 4.7 30.9 0.4 C3A C:ZNH202 4.7 34.5 0.4

Zinc binding site 8 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:25.0 occ:0.24 OE2 D:GLU127 2.0 36.6 1.0 ND1 D:HIS54 2.0 18.4 1.0 OE1 D:GLU18 2.2 23.9 1.0 OE2 D:GLU51 2.2 29.9 1.0 OE2 D:GLU18 2.4 25.3 1.0 CD D:GLU51 2.6 29.3 1.0 CD D:GLU18 2.6 23.2 1.0 OE1 D:GLU51 2.6 36.6 1.0 CE1 D:HIS54 2.9 18.4 1.0 CD D:GLU127 2.9 32.9 1.0 OE1 D:GLU127 3.1 36.3 1.0 CG D:HIS54 3.2 16.9 1.0 CB D:HIS54 3.6 16.1 1.0 CG D:GLU51 3.9 22.6 1.0 CA D:GLU51 3.9 18.0 1.0 NE2 D:HIS54 4.0 17.0 1.0 CG D:GLU18 4.1 20.1 1.0 CB D:GLU51 4.1 19.9 1.0 CD2 D:HIS54 4.2 17.0 1.0 CG D:GLU127 4.2 24.8 1.0 CG2 D:ILE123 4.3 15.4 1.0 O D:HOH447 4.4 35.0 1.0 N D:GLU51 4.7 17.9 1.0 O D:ASP50 4.8 17.8 1.0 O D:GLU51 4.8 17.1 1.0 O D:HOH322 4.8 18.6 1.0 CB D:GLU18 4.9 18.0 1.0 C D:GLU51 4.9 16.5 1.0

Zinc binding site 9 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn201 b:24.2 occ:0.24 OE1 E:GLU51 1.8 30.1 1.0 OE2 E:GLU127 1.9 37.2 1.0 ND1 E:HIS54 2.1 18.7 1.0 OE1 E:GLU18 2.2 25.2 1.0 OE2 E:GLU18 2.3 28.0 1.0 CD E:GLU18 2.5 25.1 1.0 CD E:GLU51 2.5 28.9 1.0 OE2 E:GLU51 2.8 38.0 1.0 CE1 E:HIS54 2.9 19.1 1.0 CD E:GLU127 2.9 33.0 1.0 CG E:HIS54 3.2 17.4 1.0 OE1 E:GLU127 3.3 36.0 1.0 CB E:HIS54 3.7 15.7 1.0 CG E:GLU51 3.8 22.7 1.0 CA E:GLU51 3.9 17.3 1.0 CG E:GLU18 4.0 21.1 1.0 NE2 E:HIS54 4.1 19.8 1.0 CB E:GLU51 4.1 20.2 1.0 CG E:GLU127 4.2 25.4 1.0 CD2 E:HIS54 4.2 18.6 1.0 CG2 E:ILE123 4.4 15.8 1.0 O E:HOH449 4.5 35.0 1.0 N E:GLU51 4.7 19.0 1.0 O E:ASP50 4.8 22.2 1.0 O E:HOH318 4.8 23.2 1.0 CB E:GLU18 4.8 19.1 1.0 O E:GLU51 4.9 17.2 1.0 C E:GLU51 4.9 16.7 1.0

Zinc binding site 10 out of 24 in the Escherichia Coli Bacterioferritin Substituted with Zinc Protoporphyrin IX


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 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn202 b:32.1 occ:0.27 ZN E:ZNH202 0.0 32.1 0.3 ZN E:ZNH202 0.1 31.6 0.3 ND E:ZNH202 2.1 34.2 0.4 NC E:ZNH202 2.1 32.6 0.4 NC E:ZNH202 2.2 33.2 0.4 NA E:ZNH202 2.2 34.6 0.4 ND E:ZNH202 2.2 34.3 0.4 NB E:ZNH202 2.2 33.2 0.4 NB E:ZNH202 2.3 32.2 0.4 NA E:ZNH202 2.3 33.7 0.4 SD F:MET52 2.4 25.6 1.0 SD E:MET52 2.4 25.9 1.0 C1D E:ZNH202 3.1 35.2 0.4 C4C E:ZNH202 3.1 33.3 0.4 C1C E:ZNH202 3.1 32.3 0.4 C4D E:ZNH202 3.1 35.3 0.4 C1C E:ZNH202 3.1 33.2 0.4 C4D E:ZNH202 3.1 35.1 0.4 C1A E:ZNH202 3.2 35.6 0.4 C4B E:ZNH202 3.2 33.4 0.4 C4A E:ZNH202 3.2 35.7 0.4 C4C E:ZNH202 3.2 33.6 0.4 C1B E:ZNH202 3.2 34.0 0.4 C1D E:ZNH202 3.2 34.5 0.4 C4B E:ZNH202 3.2 31.8 0.4 C1A E:ZNH202 3.2 34.6 0.4 CE E:MET52 3.2 27.3 1.0 CE F:MET52 3.2 24.9 1.0 C4A E:ZNH202 3.3 33.6 0.4 C1B E:ZNH202 3.3 32.3 0.4 CHD E:ZNH202 3.4 34.5 0.4 CHC E:ZNH202 3.5 31.9 0.4 CHC E:ZNH202 3.5 33.5 0.4 CHA E:ZNH202 3.5 34.7 0.4 CHA E:ZNH202 3.5 35.1 0.4 CHB E:ZNH202 3.5 35.3 0.4 CHD E:ZNH202 3.5 34.2 0.4 CG E:MET52 3.5 19.7 1.0 CG F:MET52 3.6 18.3 1.0 CHB E:ZNH202 3.7 33.1 0.4 CB E:MET52 4.3 18.7 1.0 CB F:MET52 4.4 17.2 1.0 C3C E:ZNH202 4.4 32.8 0.4 C2D E:ZNH202 4.4 36.1 0.4 C3D E:ZNH202 4.4 36.7 0.4 C2C E:ZNH202 4.4 32.4 0.4 C3C E:ZNH202 4.5 32.8 0.4 C3D E:ZNH202 4.5 36.3 0.4 C2C E:ZNH202 4.5 32.5 0.4 C3B E:ZNH202 4.5 33.0 0.4 C2A E:ZNH202 4.5 36.9 0.4 C2D E:ZNH202 4.5 35.1 0.4 C3A E:ZNH202 4.5 36.2 0.4 C2B E:ZNH202 4.5 33.4 0.4 C3B E:ZNH202 4.5 30.3 0.4 C2A E:ZNH202 4.5 35.8 0.4 C3A E:ZNH202 4.6 34.1 0.4 C2B E:ZNH202 4.6 31.0 0.4

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