Iron 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:

Zinc

(Zn)

2 atoms

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

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Escherichia Coli Bacterioferritin Mutant E128R/E135R within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe203 b:14.6 occ:0.50 FE A:HEM203 0.0 14.6 0.5 FE A:HEM204 0.8 11.2 0.5 NA A:HEM204 1.4 10.2 0.5 NB A:HEM204 1.8 10.1 0.5 ND A:HEM203 2.0 14.5 0.5 NA A:HEM203 2.0 13.7 0.5 NC A:HEM203 2.0 13.5 0.5 NB A:HEM203 2.1 13.1 0.5 C4A A:HEM204 2.3 9.7 0.5 SD B:MET52 2.3 16.8 1.0 SD A:MET52 2.4 15.2 1.0 C1B A:HEM204 2.5 9.1 0.5 ND A:HEM204 2.5 11.5 0.5 C1A A:HEM204 2.7 9.8 0.5 NC A:HEM204 2.7 10.9 0.5 CHB A:HEM204 2.7 8.8 0.5 C4D A:HEM203 3.0 14.6 0.5 C1D A:HEM203 3.0 14.7 0.5 C4B A:HEM204 3.0 9.0 0.5 C1A A:HEM203 3.1 14.8 0.5 C4C A:HEM203 3.1 14.7 0.5 C4A A:HEM203 3.1 14.8 0.5 C1C A:HEM203 3.1 14.1 0.5 C1B A:HEM203 3.1 13.0 0.5 C4B A:HEM203 3.1 13.2 0.5 CE A:MET52 3.2 14.2 1.0 C4D A:HEM204 3.3 11.1 0.5 CHA A:HEM204 3.3 10.7 0.5 CG B:MET52 3.3 18.5 1.0 CHA A:HEM203 3.4 14.8 0.5 CHD A:HEM203 3.4 14.2 0.5 CHB A:HEM203 3.4 12.9 0.5 CHC A:HEM203 3.5 13.0 0.5 C1C A:HEM204 3.6 10.4 0.5 C3A A:HEM204 3.6 10.0 0.5 CE B:MET52 3.6 17.1 1.0 CG A:MET52 3.6 15.7 1.0 CHC A:HEM204 3.7 9.7 0.5 C1D A:HEM204 3.7 12.6 0.5 C2A A:HEM204 3.7 11.7 0.5 C4C A:HEM204 3.8 12.3 0.5 C2B A:HEM204 3.9 9.6 0.5 CB B:MET52 3.9 18.3 1.0 C3B A:HEM204 4.1 10.7 0.5 CHD A:HEM204 4.2 13.1 0.5 C3D A:HEM203 4.2 15.6 0.5 C2D A:HEM203 4.3 14.7 0.5 C2A A:HEM203 4.3 16.4 0.5 C3C A:HEM203 4.3 15.5 0.5 C3A A:HEM203 4.3 14.4 0.5 C2C A:HEM203 4.3 14.7 0.5 C2B A:HEM203 4.3 12.5 0.5 C3B A:HEM203 4.4 14.0 0.5 CB A:MET52 4.4 15.6 1.0 C3D A:HEM204 4.6 12.8 0.5 CD1 A:ILE49 4.8 20.1 1.0 C2D A:HEM204 4.9 11.8 0.5 C2C A:HEM204 4.9 12.5 0.5 CMA A:HEM204 5.0 10.8 0.5 C3C A:HEM204 5.0 11.8 0.5

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Escherichia Coli Bacterioferritin Mutant E128R/E135R within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe204 b:11.2 occ:0.50 FE A:HEM204 0.0 11.2 0.5 FE A:HEM203 0.8 14.6 0.5 NB A:HEM203 1.5 13.1 0.5 NA A:HEM203 1.8 13.7 0.5 NB A:HEM204 2.0 10.1 0.5 NC A:HEM204 2.0 10.9 0.5 NA A:HEM204 2.1 10.2 0.5 ND A:HEM204 2.1 11.5 0.5 SD B:MET52 2.3 16.8 1.0 C1B A:HEM203 2.4 13.0 0.5 SD A:MET52 2.4 15.2 1.0 NC A:HEM203 2.5 13.5 0.5 C4A A:HEM203 2.5 14.8 0.5 C4B A:HEM203 2.7 13.2 0.5 ND A:HEM203 2.7 14.5 0.5 CHB A:HEM203 2.7 12.9 0.5 C1C A:HEM204 3.0 10.4 0.5 C1A A:HEM203 3.0 14.8 0.5 C4B A:HEM204 3.1 9.0 0.5 C4C A:HEM204 3.1 12.3 0.5 C1B A:HEM204 3.1 9.1 0.5 C1A A:HEM204 3.1 9.8 0.5 C4A A:HEM204 3.1 9.7 0.5 C1D A:HEM204 3.1 12.6 0.5 C4D A:HEM204 3.1 11.1 0.5 CE B:MET52 3.2 17.1 1.0 C1C A:HEM203 3.2 14.1 0.5 CHC A:HEM203 3.3 13.0 0.5 CG A:MET52 3.4 15.7 1.0 CHC A:HEM204 3.4 9.7 0.5 CHD A:HEM204 3.4 13.1 0.5 CHA A:HEM204 3.4 10.7 0.5 CHB A:HEM204 3.5 8.8 0.5 CG B:MET52 3.5 18.5 1.0 CE A:MET52 3.5 14.2 1.0 C4D A:HEM203 3.5 14.6 0.5 C2B A:HEM203 3.6 12.5 0.5 C4C A:HEM203 3.6 14.7 0.5 CHA A:HEM203 3.7 14.8 0.5 C3B A:HEM203 3.8 14.0 0.5 C1D A:HEM203 3.8 14.7 0.5 C3A A:HEM203 3.9 14.4 0.5 CB A:MET52 4.0 15.6 1.0 C2A A:HEM203 4.1 16.4 0.5 CHD A:HEM203 4.1 14.2 0.5 C2C A:HEM204 4.3 12.5 0.5 C3B A:HEM204 4.3 10.7 0.5 C3C A:HEM204 4.3 11.8 0.5 C2B A:HEM204 4.3 9.6 0.5 CB B:MET52 4.3 18.3 1.0 C2A A:HEM204 4.3 11.7 0.5 C3A A:HEM204 4.3 10.0 0.5 C3D A:HEM204 4.3 12.8 0.5 C2D A:HEM204 4.3 11.8 0.5 C2C A:HEM203 4.6 14.7 0.5 C3C A:HEM203 4.8 15.5 0.5 C3D A:HEM203 4.9 15.6 0.5 CMB A:HEM203 5.0 14.1 0.5 C2D A:HEM203 5.0 14.7 0.5

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