Atomistry » Iron » PDB 3e13-3eai » 3e1l
Atomistry »
  Iron »
    PDB 3e13-3eai »
      3e1l »

Iron in PDB 3e1l: Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).

Protein crystallography data

The structure of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II)., PDB code: 3e1l was solved by A.Crow, T.Lawson, A.Lewin, G.R.Moore, N.Le Brun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 2.50
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 208.082, 208.082, 143.107, 90.00, 90.00, 90.00
R / Rfree (%) 23.6 / 24.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). (pdb code 3e1l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II)., PDB code: 3e1l:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 1 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe200

b:2.0
occ:0.04
FE A:HEM200 0.0 2.0 0.0
NC A:HEM200 2.1 2.0 0.0
SD A:MET52 2.1 19.3 1.0
NB A:HEM200 2.1 2.0 0.0
NA A:HEM200 2.1 2.0 0.0
ND A:HEM200 2.1 2.0 0.0
SD B:MET52 2.1 19.3 1.0
CE A:MET52 3.1 17.9 1.0
C1C A:HEM200 3.1 2.0 0.0
C4C A:HEM200 3.1 2.0 0.0
CE B:MET52 3.1 17.9 1.0
C4B A:HEM200 3.1 2.0 0.0
C1D A:HEM200 3.1 2.0 0.0
C1A A:HEM200 3.1 2.0 0.0
C4D A:HEM200 3.1 2.0 0.0
C1B A:HEM200 3.1 2.0 0.0
C4A A:HEM200 3.1 2.0 0.0
CHC A:HEM200 3.4 2.0 0.0
CHD A:HEM200 3.4 2.0 0.0
CG A:MET52 3.5 16.2 1.0
CHA A:HEM200 3.5 2.0 0.0
CHB A:HEM200 3.5 2.0 0.0
CG B:MET52 3.5 16.2 1.0
CB A:MET52 4.3 14.5 1.0
C2C A:HEM200 4.3 2.0 0.0
C3C A:HEM200 4.3 2.0 0.0
C3B A:HEM200 4.3 2.0 0.0
C2B A:HEM200 4.3 2.0 0.0
CB B:MET52 4.3 14.5 1.0
C2A A:HEM200 4.3 2.0 0.0
C3A A:HEM200 4.3 2.0 0.0
C2D A:HEM200 4.4 2.0 0.0
C3D A:HEM200 4.4 2.0 0.0

Iron binding site 2 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 2 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe200

b:2.0
occ:0.04
FE C:HEM200 0.0 2.0 0.0
SD D:MET52 2.1 19.3 1.0
NC C:HEM200 2.1 2.0 0.0
NB C:HEM200 2.1 2.0 0.0
NA C:HEM200 2.1 2.0 0.0
SD C:MET52 2.1 19.3 1.0
ND C:HEM200 2.1 2.0 0.0
CE D:MET52 3.1 17.9 1.0
C1C C:HEM200 3.1 2.0 0.0
C4B C:HEM200 3.1 2.0 0.0
CE C:MET52 3.1 17.9 1.0
C4C C:HEM200 3.1 2.0 0.0
C1B C:HEM200 3.1 2.0 0.0
C1A C:HEM200 3.1 2.0 0.0
C4D C:HEM200 3.1 2.0 0.0
C1D C:HEM200 3.1 2.0 0.0
C4A C:HEM200 3.1 2.0 0.0
CHC C:HEM200 3.4 2.0 0.0
CG D:MET52 3.4 16.2 1.0
CHD C:HEM200 3.5 2.0 0.0
CHA C:HEM200 3.5 2.0 0.0
CHB C:HEM200 3.5 2.0 0.0
CG C:MET52 3.5 16.2 1.0
CB D:MET52 4.2 14.5 1.0
C2C C:HEM200 4.3 2.0 0.0
C3B C:HEM200 4.3 2.0 0.0
C3C C:HEM200 4.3 2.0 0.0
C2B C:HEM200 4.3 2.0 0.0
CB C:MET52 4.3 14.5 1.0
C2A C:HEM200 4.3 2.0 0.0
C3A C:HEM200 4.3 2.0 0.0
C3D C:HEM200 4.4 2.0 0.0
C2D C:HEM200 4.4 2.0 0.0

Iron binding site 3 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 3 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe200

b:2.0
occ:0.04
FE E:HEM200 0.0 2.0 0.0
SD E:MET52 2.0 19.3 1.0
SD F:MET52 2.1 19.3 1.0
NC E:HEM200 2.1 2.0 0.0
NA E:HEM200 2.1 2.0 0.0
ND E:HEM200 2.1 2.0 0.0
NB E:HEM200 2.1 2.0 0.0
CE E:MET52 3.1 17.9 1.0
CE F:MET52 3.1 17.9 1.0
C1A E:HEM200 3.1 2.0 0.0
C1C E:HEM200 3.1 2.0 0.0
C4C E:HEM200 3.1 2.0 0.0
C4D E:HEM200 3.1 2.0 0.0
C1D E:HEM200 3.1 2.0 0.0
C4B E:HEM200 3.1 2.0 0.0
C4A E:HEM200 3.1 2.0 0.0
C1B E:HEM200 3.1 2.0 0.0
CHA E:HEM200 3.4 2.0 0.0
CHD E:HEM200 3.4 2.0 0.0
CHC E:HEM200 3.5 2.0 0.0
CHB E:HEM200 3.5 2.0 0.0
CG F:MET52 3.5 16.2 1.0
CG E:MET52 3.5 16.2 1.0
CB F:MET52 4.3 14.5 1.0
CB E:MET52 4.3 14.5 1.0
C2C E:HEM200 4.3 2.0 0.0
C3C E:HEM200 4.3 2.0 0.0
C2A E:HEM200 4.3 2.0 0.0
C3A E:HEM200 4.3 2.0 0.0
C3D E:HEM200 4.3 2.0 0.0
C2D E:HEM200 4.3 2.0 0.0
C3B E:HEM200 4.3 2.0 0.0
C2B E:HEM200 4.4 2.0 0.0
CD1 E:ILE49 4.9 16.3 1.0
CD1 F:ILE49 4.9 16.3 1.0

Iron binding site 4 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 4 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe200

b:2.0
occ:0.04
FE G:HEM200 0.0 2.0 0.0
NC G:HEM200 2.1 2.0 0.0
SD H:MET52 2.1 19.3 1.0
SD G:MET52 2.1 19.3 1.0
NB G:HEM200 2.1 2.0 0.0
NA G:HEM200 2.1 2.0 0.0
ND G:HEM200 2.1 2.0 0.0
CE G:MET52 3.1 17.9 1.0
C1C G:HEM200 3.1 2.0 0.0
C4B G:HEM200 3.1 2.0 0.0
C4C G:HEM200 3.1 2.0 0.0
CE H:MET52 3.1 17.9 1.0
C1A G:HEM200 3.1 2.0 0.0
C1B G:HEM200 3.1 2.0 0.0
C4D G:HEM200 3.1 2.0 0.0
C4A G:HEM200 3.1 2.0 0.0
C1D G:HEM200 3.1 2.0 0.0
CHC G:HEM200 3.4 2.0 0.0
CHA G:HEM200 3.5 2.0 0.0
CHD G:HEM200 3.5 2.0 0.0
CG H:MET52 3.5 16.2 1.0
CHB G:HEM200 3.5 2.0 0.0
CG G:MET52 3.5 16.2 1.0
CB H:MET52 4.2 14.4 1.0
C2C G:HEM200 4.3 2.0 0.0
C3C G:HEM200 4.3 2.0 0.0
CB G:MET52 4.3 14.5 1.0
C3B G:HEM200 4.3 2.0 0.0
C2B G:HEM200 4.3 2.0 0.0
C2A G:HEM200 4.3 2.0 0.0
C3A G:HEM200 4.3 2.0 0.0
C3D G:HEM200 4.4 2.0 0.0
C2D G:HEM200 4.4 2.0 0.0
CD1 G:ILE49 5.0 16.3 1.0
CD1 H:ILE49 5.0 16.3 1.0

Iron binding site 5 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 5 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe200

b:2.0
occ:0.04
FE I:HEM200 0.0 2.0 0.0
SD I:MET52 2.1 19.3 1.0
NC I:HEM200 2.1 2.0 0.0
SD J:MET52 2.1 19.3 1.0
NB I:HEM200 2.1 2.0 0.0
NA I:HEM200 2.1 2.0 0.0
ND I:HEM200 2.1 2.0 0.0
CE I:MET52 3.0 17.9 1.0
C1C I:HEM200 3.1 2.0 0.0
CE J:MET52 3.1 17.9 1.0
C4B I:HEM200 3.1 2.0 0.0
C4C I:HEM200 3.1 2.0 0.0
C1A I:HEM200 3.1 2.0 0.0
C4D I:HEM200 3.1 2.0 0.0
C1B I:HEM200 3.1 2.0 0.0
C4A I:HEM200 3.1 2.0 0.0
C1D I:HEM200 3.1 2.0 0.0
CHC I:HEM200 3.4 2.0 0.0
CHA I:HEM200 3.4 2.0 0.0
CHD I:HEM200 3.5 2.0 0.0
CG I:MET52 3.5 16.2 1.0
CHB I:HEM200 3.5 2.0 0.0
CG J:MET52 3.5 16.2 1.0
CB J:MET52 4.3 14.5 1.0
CB I:MET52 4.3 14.5 1.0
C2C I:HEM200 4.3 2.0 0.0
C3C I:HEM200 4.3 2.0 0.0
C3B I:HEM200 4.3 2.0 0.0
C2A I:HEM200 4.3 2.0 0.0
C2B I:HEM200 4.3 2.0 0.0
C3A I:HEM200 4.3 2.0 0.0
C3D I:HEM200 4.4 2.0 0.0
C2D I:HEM200 4.4 2.0 0.0
CD1 I:ILE49 5.0 16.3 1.0
CD1 J:ILE49 5.0 16.3 1.0

Iron binding site 6 out of 6 in 3e1l

Go back to Iron Binding Sites List in 3e1l
Iron binding site 6 out of 6 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of E. Coli Bacterioferritin (Bfr) Soaked in Phosphate with An Alternative Conformation of the Unoccupied Ferroxidase Centre (Apo-Bfr II). within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Fe200

b:2.0
occ:0.04
FE K:HEM200 0.0 2.0 0.0
SD K:MET52 2.1 19.3 1.0
SD L:MET52 2.1 19.3 1.0
NC K:HEM200 2.2 2.0 0.0
NB K:HEM200 2.2 2.0 0.0
ND K:HEM200 2.2 2.0 0.0
NA K:HEM200 2.2 2.0 0.0
CE K:MET52 3.1 17.9 1.0
CE L:MET52 3.1 17.9 1.0
C1C K:HEM200 3.2 2.0 0.0
C4B K:HEM200 3.2 2.0 0.0
C4D K:HEM200 3.2 2.0 0.0
C4C K:HEM200 3.2 2.0 0.0
C1B K:HEM200 3.2 2.0 0.0
C1D K:HEM200 3.2 2.0 0.0
C4A K:HEM200 3.2 2.0 0.0
C1A K:HEM200 3.2 2.0 0.0
CHC K:HEM200 3.5 2.0 0.0
CG L:MET52 3.5 16.2 1.0
CG K:MET52 3.5 16.2 1.0
CHD K:HEM200 3.6 2.0 0.0
CHB K:HEM200 3.6 2.0 0.0
CB L:MET52 4.3 14.5 1.0
CB K:MET52 4.3 14.5 1.0
C2C K:HEM200 4.4 2.0 0.0
C3B K:HEM200 4.4 2.0 0.0
C3C K:HEM200 4.4 2.0 0.0
C2B K:HEM200 4.4 2.0 0.0
C3D K:HEM200 4.4 2.0 0.0
C3A K:HEM200 4.5 2.0 0.0
C2D K:HEM200 4.5 2.0 0.0
C2A K:HEM200 4.5 2.0 0.0
CD1 K:ILE49 4.9 16.3 1.0
CD1 L:ILE49 5.0 16.3 1.0

Reference:

A.Crow, T.L.Lawson, A.Lewin, G.R.Moore, N.E.Le Brun. Structural Basis For Iron Mineralization By Bacterioferritin J.Am.Chem.Soc. V. 131 6808 2009.
ISSN: ISSN 0002-7863
PubMed: 19391621
DOI: 10.1021/JA8093444
Page generated: Tue Aug 5 00:43:23 2025

Last articles

Xe in 1RJO
Xe in 1O75
Xe in 1NXT
Xe in 1LLS
Xe in 1L1G
Xe in 1L0Z
Xe in 1E9V
Xe in 1K4K
Xe in 1FZH
Xe in 1J52
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy