Zinc in PDB 3e2c: Escherichia Coli Bacterioferritin Mutant E128R/E135R

All present enzymatic activity of Escherichia Coli Bacterioferritin Mutant E128R/E135R:
1.16.3.1;

The structure of Escherichia Coli Bacterioferritin Mutant E128R/E135R, PDB code: 3e2c was solved by S.G.Wong, S.A.L.Tom-Yew, A.Lewin, N.E.Le Brun, G.R.Moore, M.E.P.Murphy, A.G.Mauk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.54 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.639, 91.089, 102.085, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 22.8

The structure of Escherichia Coli Bacterioferritin Mutant E128R/E135R also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Zinc atom in the Escherichia Coli Bacterioferritin Mutant E128R/E135R (pdb code 3e2c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Escherichia Coli Bacterioferritin Mutant E128R/E135R, PDB code: 3e2c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Escherichia Coli Bacterioferritin Mutant E128R/E135R


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 Mutant E128R/E135R within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn200 b:18.4 occ:1.00 OE1 A:GLU51 1.8 20.4 1.0 OE1 A:GLU18 1.9 22.4 1.0 OE2 A:GLU127 2.0 17.7 1.0 ND1 A:HIS54 2.1 18.3 1.0 CD A:GLU127 2.8 17.0 1.0 CD A:GLU18 2.8 19.9 1.0 CD A:GLU51 2.9 20.2 1.0 OE1 A:GLU127 2.9 20.9 1.0 CE1 A:HIS54 3.0 17.6 1.0 OE2 A:GLU18 3.0 20.4 1.0 CG A:HIS54 3.1 16.3 1.0 OE2 A:GLU51 3.4 22.1 1.0 CB A:HIS54 3.5 16.6 1.0 O A:HOH315 3.9 24.9 1.0 CG2 A:ILE123 4.1 18.0 1.0 CG A:GLU127 4.1 16.7 1.0 NE2 A:HIS54 4.1 17.1 1.0 CG A:GLU18 4.1 17.6 1.0 O2 A:EDO301 4.2 24.2 1.0 CD2 A:HIS54 4.2 16.9 1.0 O1 A:EDO302 4.2 27.8 1.0 CG A:GLU51 4.2 16.5 1.0 CA A:GLU51 4.3 15.4 1.0 O1 A:EDO301 4.4 22.5 1.0 C2 A:EDO302 4.5 25.2 1.0 CB A:GLU51 4.6 15.2 1.0 C2 A:EDO301 4.8 24.9 1.0 C1 A:EDO302 4.9 22.3 1.0 CB A:GLU18 4.9 16.6 1.0 O A:GLU51 5.0 15.4 1.0 CA A:HIS54 5.0 16.1 1.0

Zinc binding site 2 out of 2 in the Escherichia Coli Bacterioferritin Mutant E128R/E135R


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 Mutant E128R/E135R within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn200 b:21.4 occ:1.00 OE1 B:GLU51 1.8 22.5 1.0 OE2 B:GLU18 2.0 24.8 1.0 OE2 B:GLU127 2.0 21.1 1.0 ND1 B:HIS54 2.0 20.8 1.0 CD B:GLU18 2.8 22.4 1.0 CD B:GLU127 2.8 22.4 1.0 CD B:GLU51 2.9 21.5 1.0 OE1 B:GLU18 3.0 26.2 1.0 CE1 B:HIS54 3.0 22.7 1.0 OE1 B:GLU127 3.0 24.3 1.0 CG B:HIS54 3.0 19.8 1.0 OE2 B:GLU51 3.4 24.7 1.0 CB B:HIS54 3.4 18.0 1.0 CG2 B:ILE123 4.0 20.2 1.0 O B:HOH309 4.0 24.9 1.0 O1 B:EDO301 4.1 25.9 1.0 NE2 B:HIS54 4.1 23.2 1.0 CD2 B:HIS54 4.2 20.4 1.0 CG B:GLU18 4.2 19.4 1.0 CG B:GLU51 4.2 19.6 1.0 CG B:GLU127 4.2 26.1 1.0 CA B:GLU51 4.3 18.2 1.0 O1 B:EDO302 4.4 33.5 1.0 O2 B:EDO301 4.5 28.8 1.0 CB B:GLU51 4.5 18.7 1.0 C2 B:EDO302 4.7 30.7 1.0 C1 B:EDO301 4.9 27.4 1.0 CA B:HIS54 4.9 17.7 1.0 O B:GLU51 5.0 17.2 1.0 CB B:GLU18 5.0 16.9 1.0

S.G.Wong, S.A.Tom-Yew, A.Lewin, N.E.Le Brun, G.R.Moore, M.E.Murphy, A.G.Mauk. Structural and Mechanistic Studies of A Stabilized Subunit Dimer Variant of Escherichia Coli Bacterioferritin Identify Residues Required For Core Formation. J.Biol.Chem. V. 284 18873 2009.
ISSN: ISSN 0021-9258
PubMed: 19439409
DOI: 10.1074/JBC.M901747200