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Iron in PDB 4e6k: 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)

Protein crystallography data

The structure of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd), PDB code: 4e6k was solved by S.Lovell, K.P.Battaile, H.Yao, Y.Wang, R.Kumar, A.Ruvinsky, I.Vasker, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.73 / 2.00
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 135.005, 135.005, 200.890, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 18.3

Other elements in 4e6k:

The structure of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) also contains other interesting chemical elements:

Potassium (K) 3 atoms
Sodium (Na) 6 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Iron atom in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) (pdb code 4e6k). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd), PDB code: 4e6k:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in 4e6k

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Iron binding site 1 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:20.9
occ:0.50
FE A:HEM202 0.0 20.9 0.5
FE A:HEM202 0.2 20.6 0.5
NC A:HEM202 2.0 20.7 0.5
ND A:HEM202 2.0 19.8 0.5
NA A:HEM202 2.0 19.9 0.5
NB A:HEM202 2.0 20.5 0.5
NC A:HEM202 2.1 21.8 0.5
ND A:HEM202 2.1 22.4 0.5
NA A:HEM202 2.1 22.0 0.5
NB A:HEM202 2.2 21.8 0.5
SD B:MET52 2.3 17.4 1.0
SD A:MET52 2.3 16.9 1.0
C4C A:HEM202 3.0 19.2 0.5
C1D A:HEM202 3.0 21.7 0.5
C4D A:HEM202 3.0 21.4 0.5
C1C A:HEM202 3.0 20.6 0.5
C1A A:HEM202 3.0 21.4 0.5
C4B A:HEM202 3.0 21.0 0.5
C1C A:HEM202 3.1 20.8 0.5
C1A A:HEM202 3.1 21.4 0.5
C4D A:HEM202 3.1 21.4 0.5
C4A A:HEM202 3.1 21.8 0.5
C1B A:HEM202 3.1 19.3 0.5
C4C A:HEM202 3.1 20.2 0.5
C1D A:HEM202 3.1 22.6 0.5
C4B A:HEM202 3.2 21.0 0.5
C4A A:HEM202 3.2 22.7 0.5
CE A:MET52 3.2 17.3 1.0
CE B:MET52 3.2 20.1 1.0
C1B A:HEM202 3.3 20.2 0.5
CHD A:HEM202 3.3 20.8 0.5
CHA A:HEM202 3.4 21.0 0.5
CHC A:HEM202 3.4 19.9 0.5
CHA A:HEM202 3.4 21.0 0.5
CG B:MET52 3.4 14.9 1.0
CHC A:HEM202 3.5 19.9 0.5
CHD A:HEM202 3.5 20.4 0.5
CHB A:HEM202 3.5 20.4 0.5
CG A:MET52 3.5 15.3 1.0
CHB A:HEM202 3.6 20.2 0.5
CB B:MET52 4.2 12.4 1.0
C3C A:HEM202 4.2 20.5 0.5
C2D A:HEM202 4.2 20.2 0.5
C3D A:HEM202 4.2 22.7 0.5
C2C A:HEM202 4.2 19.8 0.5
C2A A:HEM202 4.3 22.6 0.5
C3B A:HEM202 4.3 20.0 0.5
C3A A:HEM202 4.3 20.1 0.5
C2C A:HEM202 4.3 21.8 0.5
C2B A:HEM202 4.3 20.3 0.5
C3D A:HEM202 4.3 21.5 0.5
C3C A:HEM202 4.3 20.2 0.5
C2A A:HEM202 4.3 21.4 0.5
CB A:MET52 4.3 16.9 1.0
C2D A:HEM202 4.3 19.3 0.5
C3A A:HEM202 4.4 19.3 0.5
C3B A:HEM202 4.4 21.9 0.5
C2B A:HEM202 4.5 20.1 0.5

Iron binding site 2 out of 12 in 4e6k

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Iron binding site 2 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:20.6
occ:0.50
FE A:HEM202 0.0 20.6 0.5
FE A:HEM202 0.2 20.9 0.5
NC A:HEM202 1.9 21.8 0.5
ND A:HEM202 2.0 22.4 0.5
NA A:HEM202 2.0 22.0 0.5
NC A:HEM202 2.0 20.7 0.5
NB A:HEM202 2.1 21.8 0.5
ND A:HEM202 2.1 19.8 0.5
NB A:HEM202 2.1 20.5 0.5
NA A:HEM202 2.2 19.9 0.5
SD A:MET52 2.3 16.9 1.0
SD B:MET52 2.3 17.4 1.0
C4C A:HEM202 2.9 20.2 0.5
C1C A:HEM202 3.0 20.8 0.5
C1D A:HEM202 3.0 22.6 0.5
C1A A:HEM202 3.0 21.4 0.5
C4D A:HEM202 3.0 21.4 0.5
C1C A:HEM202 3.1 20.6 0.5
C4A A:HEM202 3.1 22.7 0.5
C4D A:HEM202 3.1 21.4 0.5
C4C A:HEM202 3.1 19.2 0.5
C4B A:HEM202 3.1 21.0 0.5
C4B A:HEM202 3.1 21.0 0.5
C1B A:HEM202 3.1 20.2 0.5
C1D A:HEM202 3.1 21.7 0.5
C1A A:HEM202 3.1 21.4 0.5
CE B:MET52 3.2 20.1 1.0
C1B A:HEM202 3.2 19.3 0.5
CE A:MET52 3.2 17.3 1.0
C4A A:HEM202 3.2 21.8 0.5
CHD A:HEM202 3.3 20.4 0.5
CHC A:HEM202 3.4 19.9 0.5
CHA A:HEM202 3.4 21.0 0.5
CG A:MET52 3.4 15.3 1.0
CHC A:HEM202 3.4 19.9 0.5
CHA A:HEM202 3.4 21.0 0.5
CHB A:HEM202 3.5 20.2 0.5
CHD A:HEM202 3.5 20.8 0.5
CG B:MET52 3.6 14.9 1.0
CHB A:HEM202 3.6 20.4 0.5
C3C A:HEM202 4.2 20.2 0.5
C2C A:HEM202 4.2 21.8 0.5
CB A:MET52 4.2 16.9 1.0
C2D A:HEM202 4.2 19.3 0.5
C2A A:HEM202 4.2 21.4 0.5
C3D A:HEM202 4.2 21.5 0.5
C3A A:HEM202 4.3 19.3 0.5
C2C A:HEM202 4.3 19.8 0.5
C3C A:HEM202 4.3 20.5 0.5
C3B A:HEM202 4.3 21.9 0.5
CB B:MET52 4.3 12.4 1.0
C2B A:HEM202 4.3 20.1 0.5
C3D A:HEM202 4.3 22.7 0.5
C2D A:HEM202 4.3 20.2 0.5
C3B A:HEM202 4.4 20.0 0.5
C2A A:HEM202 4.4 22.6 0.5
C2B A:HEM202 4.4 20.3 0.5
C3A A:HEM202 4.4 20.1 0.5

Iron binding site 3 out of 12 in 4e6k

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Iron binding site 3 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:20.9
occ:0.50
FE C:HEM201 0.0 20.9 0.5
FE C:HEM201 0.7 21.6 0.5
SD C:MET52 2.0 18.5 1.0
ND C:HEM201 2.0 21.1 0.5
NA C:HEM201 2.1 22.5 0.5
NC C:HEM201 2.1 22.2 0.5
NB C:HEM201 2.1 21.7 0.5
NC C:HEM201 2.1 22.3 0.5
NA C:HEM201 2.1 22.2 0.5
ND C:HEM201 2.2 22.2 0.5
NB C:HEM201 2.2 21.5 0.5
SD D:MET52 2.7 20.6 1.0
C1D C:HEM201 3.0 21.4 0.5
CE C:MET52 3.0 18.7 1.0
C4D C:HEM201 3.1 23.3 0.5
C1A C:HEM201 3.1 22.9 0.5
C4C C:HEM201 3.1 23.2 0.5
C4C C:HEM201 3.1 20.5 0.5
C1C C:HEM201 3.1 22.6 0.5
C1A C:HEM201 3.1 23.3 0.5
C4A C:HEM201 3.1 24.1 0.5
C1B C:HEM201 3.1 20.4 0.5
C4D C:HEM201 3.1 23.1 0.5
C1C C:HEM201 3.1 22.0 0.5
C1D C:HEM201 3.1 23.8 0.5
C4B C:HEM201 3.1 22.6 0.5
C4A C:HEM201 3.1 21.3 0.5
C4B C:HEM201 3.1 22.1 0.5
C1B C:HEM201 3.2 22.6 0.5
CG C:MET52 3.2 20.3 1.0
CHD C:HEM201 3.4 20.8 0.5
CHA C:HEM201 3.4 20.8 0.5
CHA C:HEM201 3.4 20.5 0.5
CHD C:HEM201 3.5 20.6 0.5
CHB C:HEM201 3.5 20.9 0.5
CHC C:HEM201 3.5 24.6 0.5
CHC C:HEM201 3.5 25.0 0.5
CHB C:HEM201 3.5 21.1 0.5
CE D:MET52 3.5 18.6 1.0
CG D:MET52 3.9 16.7 1.0
CB C:MET52 4.0 16.3 1.0
C2C C:HEM201 4.3 24.2 0.5
C3C C:HEM201 4.3 23.8 0.5
C2D C:HEM201 4.3 21.8 0.5
C3D C:HEM201 4.3 22.2 0.5
C2A C:HEM201 4.3 22.3 0.5
C3D C:HEM201 4.3 22.6 0.5
C3A C:HEM201 4.3 20.6 0.5
C2D C:HEM201 4.3 20.8 0.5
C3C C:HEM201 4.3 22.2 0.5
C2A C:HEM201 4.3 22.2 0.5
C2C C:HEM201 4.3 22.2 0.5
C2B C:HEM201 4.3 23.7 0.5
C3B C:HEM201 4.3 24.3 0.5
C3A C:HEM201 4.3 21.6 0.5
C3B C:HEM201 4.4 22.4 0.5
C2B C:HEM201 4.4 22.1 0.5
CB D:MET52 4.6 16.5 1.0
CD1 C:ILE49 4.9 23.1 1.0

Iron binding site 4 out of 12 in 4e6k

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Iron binding site 4 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:21.6
occ:0.50
FE C:HEM201 0.0 21.6 0.5
FE C:HEM201 0.7 20.9 0.5
NA C:HEM201 2.0 22.2 0.5
SD D:MET52 2.0 20.6 1.0
NC C:HEM201 2.1 22.3 0.5
NB C:HEM201 2.1 21.5 0.5
ND C:HEM201 2.1 21.1 0.5
NC C:HEM201 2.1 22.2 0.5
ND C:HEM201 2.1 22.2 0.5
NA C:HEM201 2.2 22.5 0.5
NB C:HEM201 2.2 21.7 0.5
SD C:MET52 2.7 18.5 1.0
CE D:MET52 3.0 18.6 1.0
C1A C:HEM201 3.0 23.3 0.5
C1D C:HEM201 3.0 21.4 0.5
C4A C:HEM201 3.0 21.3 0.5
C4C C:HEM201 3.1 23.2 0.5
C4D C:HEM201 3.1 23.3 0.5
C1C C:HEM201 3.1 22.6 0.5
C4B C:HEM201 3.1 22.1 0.5
C1B C:HEM201 3.1 22.6 0.5
C4C C:HEM201 3.1 20.5 0.5
C1C C:HEM201 3.1 22.0 0.5
C4D C:HEM201 3.1 23.1 0.5
C1D C:HEM201 3.1 23.8 0.5
C1A C:HEM201 3.1 22.9 0.5
C4B C:HEM201 3.2 22.6 0.5
C1B C:HEM201 3.2 20.4 0.5
C4A C:HEM201 3.2 24.1 0.5
CG D:MET52 3.3 16.7 1.0
CHD C:HEM201 3.4 20.8 0.5
CHA C:HEM201 3.4 20.5 0.5
CHB C:HEM201 3.4 21.1 0.5
CHC C:HEM201 3.4 24.6 0.5
CHA C:HEM201 3.5 20.8 0.5
CHD C:HEM201 3.5 20.6 0.5
CHC C:HEM201 3.5 25.0 0.5
CHB C:HEM201 3.6 20.9 0.5
CE C:MET52 3.6 18.7 1.0
CG C:MET52 3.8 20.3 1.0
CB D:MET52 4.0 16.5 1.0
C2D C:HEM201 4.2 21.8 0.5
C3D C:HEM201 4.2 22.2 0.5
C2A C:HEM201 4.2 22.2 0.5
C3C C:HEM201 4.3 22.2 0.5
C3A C:HEM201 4.3 21.6 0.5
C2C C:HEM201 4.3 22.2 0.5
C2C C:HEM201 4.3 24.2 0.5
C3B C:HEM201 4.3 22.4 0.5
C3C C:HEM201 4.3 23.8 0.5
C2B C:HEM201 4.3 22.1 0.5
C3D C:HEM201 4.4 22.6 0.5
C3B C:HEM201 4.4 24.3 0.5
C2A C:HEM201 4.4 22.3 0.5
C2B C:HEM201 4.4 23.7 0.5
C2D C:HEM201 4.4 20.8 0.5
C3A C:HEM201 4.4 20.6 0.5
CB C:MET52 4.5 16.3 1.0

Iron binding site 5 out of 12 in 4e6k

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Iron binding site 5 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe201

b:19.7
occ:0.50
FE E:HEM201 0.0 19.7 0.5
FE E:HEM201 0.5 20.1 0.5
ND E:HEM201 1.8 18.6 0.5
NC E:HEM201 1.9 18.6 0.5
NA E:HEM201 2.0 18.7 0.5
NB E:HEM201 2.1 18.3 0.5
NC E:HEM201 2.1 18.0 0.5
ND E:HEM201 2.1 20.0 0.5
SD F:MET52 2.2 16.2 1.0
NA E:HEM201 2.3 20.1 0.5
NB E:HEM201 2.4 17.8 0.5
SD E:MET52 2.5 16.8 1.0
C1D E:HEM201 2.7 19.9 0.5
C4C E:HEM201 2.8 18.4 0.5
C4D E:HEM201 2.9 21.4 0.5
C1A E:HEM201 3.0 21.6 0.5
C4A E:HEM201 3.0 20.2 0.5
C1C E:HEM201 3.0 19.4 0.5
C4D E:HEM201 3.1 20.4 0.5
CHD E:HEM201 3.1 21.0 0.5
C1C E:HEM201 3.1 18.5 0.5
C1B E:HEM201 3.1 18.6 0.5
C4B E:HEM201 3.1 20.0 0.5
C4C E:HEM201 3.1 18.8 0.5
C1D E:HEM201 3.1 19.8 0.5
C1A E:HEM201 3.2 20.6 0.5
CE F:MET52 3.2 16.4 1.0
C4B E:HEM201 3.3 18.7 0.5
CE E:MET52 3.3 17.1 1.0
CG F:MET52 3.3 13.5 1.0
CHA E:HEM201 3.4 18.8 0.5
CHA E:HEM201 3.4 18.8 0.5
C4A E:HEM201 3.4 19.7 0.5
CHB E:HEM201 3.4 21.2 0.5
CHC E:HEM201 3.5 18.8 0.5
C1B E:HEM201 3.5 18.6 0.5
CHD E:HEM201 3.5 17.8 0.5
CHC E:HEM201 3.5 18.5 0.5
CG E:MET52 3.7 16.1 1.0
CHB E:HEM201 3.8 18.1 0.5
C2D E:HEM201 4.0 18.4 0.5
CB F:MET52 4.0 13.1 1.0
C3D E:HEM201 4.0 19.9 0.5
C3C E:HEM201 4.1 19.5 0.5
C2C E:HEM201 4.2 18.3 0.5
C2A E:HEM201 4.2 19.9 0.5
C3A E:HEM201 4.2 18.1 0.5
C3D E:HEM201 4.3 21.2 0.5
C3B E:HEM201 4.3 19.0 0.5
C2B E:HEM201 4.3 18.9 0.5
C2C E:HEM201 4.3 18.5 0.5
C3C E:HEM201 4.3 18.0 0.5
C2D E:HEM201 4.4 18.8 0.5
C2A E:HEM201 4.5 21.1 0.5
CB E:MET52 4.5 15.6 1.0
C3B E:HEM201 4.6 18.8 0.5
C3A E:HEM201 4.6 18.7 0.5
C2B E:HEM201 4.7 17.3 0.5

Iron binding site 6 out of 12 in 4e6k

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Iron binding site 6 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe201

b:20.1
occ:0.50
FE E:HEM201 0.0 20.1 0.5
FE E:HEM201 0.5 19.7 0.5
NC E:HEM201 1.8 18.0 0.5
ND E:HEM201 1.9 20.0 0.5
NB E:HEM201 2.0 17.8 0.5
NA E:HEM201 2.0 20.1 0.5
NC E:HEM201 2.1 18.6 0.5
ND E:HEM201 2.1 18.6 0.5
SD E:MET52 2.3 16.8 1.0
NA E:HEM201 2.3 18.7 0.5
NB E:HEM201 2.3 18.3 0.5
SD F:MET52 2.5 16.2 1.0
C4C E:HEM201 2.7 18.8 0.5
C1D E:HEM201 2.8 19.8 0.5
C1C E:HEM201 2.9 18.5 0.5
C4D E:HEM201 3.0 20.4 0.5
C4B E:HEM201 3.0 18.7 0.5
C1B E:HEM201 3.1 18.6 0.5
C4A E:HEM201 3.1 19.7 0.5
C1A E:HEM201 3.1 20.6 0.5
CHD E:HEM201 3.1 17.8 0.5
C1C E:HEM201 3.1 19.4 0.5
C4D E:HEM201 3.1 21.4 0.5
C1D E:HEM201 3.1 19.9 0.5
C4C E:HEM201 3.1 18.4 0.5
CE F:MET52 3.2 16.4 1.0
C4B E:HEM201 3.2 20.0 0.5
C1A E:HEM201 3.3 21.6 0.5
CE E:MET52 3.3 17.1 1.0
CG E:MET52 3.3 16.1 1.0
CHC E:HEM201 3.4 18.8 0.5
CHB E:HEM201 3.4 18.1 0.5
CHC E:HEM201 3.4 18.5 0.5
C4A E:HEM201 3.4 20.2 0.5
CHA E:HEM201 3.4 18.8 0.5
C1B E:HEM201 3.5 18.6 0.5
CHD E:HEM201 3.5 21.0 0.5
CHA E:HEM201 3.5 18.8 0.5
CG F:MET52 3.7 13.5 1.0
CHB E:HEM201 3.9 21.2 0.5
C3C E:HEM201 4.0 18.0 0.5
CB E:MET52 4.0 15.6 1.0
C2C E:HEM201 4.0 18.5 0.5
C2D E:HEM201 4.1 18.8 0.5
C3D E:HEM201 4.1 21.2 0.5
C3B E:HEM201 4.3 18.8 0.5
C2B E:HEM201 4.3 17.3 0.5
C3A E:HEM201 4.3 18.7 0.5
C2A E:HEM201 4.3 21.1 0.5
C2C E:HEM201 4.3 18.3 0.5
C2D E:HEM201 4.3 18.4 0.5
C3D E:HEM201 4.3 19.9 0.5
C3C E:HEM201 4.3 19.5 0.5
CB F:MET52 4.5 13.1 1.0
C3B E:HEM201 4.5 19.0 0.5
C2A E:HEM201 4.5 19.9 0.5
C3A E:HEM201 4.6 18.1 0.5
C2B E:HEM201 4.6 18.9 0.5

Iron binding site 7 out of 12 in 4e6k

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Iron binding site 7 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe101

b:17.8
occ:1.00
FE1 G:FES101 0.0 17.8 1.0
S2 G:FES101 2.2 19.7 1.0
SG G:CYS38 2.2 19.7 1.0
S1 G:FES101 2.3 19.7 1.0
SG G:CYS6 2.3 20.8 1.0
FE2 G:FES101 2.8 18.4 1.0
CB G:CYS6 3.3 18.7 1.0
CB G:CYS38 3.4 20.9 1.0
N G:CYS38 3.5 20.5 1.0
N G:GLY39 3.8 21.7 1.0
CA G:CYS38 3.9 20.1 1.0
N G:CYS6 4.1 18.3 1.0
C G:CYS38 4.2 24.9 1.0
CA G:CYS6 4.3 15.8 1.0
N G:LYS40 4.4 20.8 1.0
CG B:GLN72 4.4 20.0 1.0
SG G:CYS4 4.4 19.6 1.0
CB G:GLN37 4.6 19.1 1.0
C G:GLN37 4.6 22.4 1.0
SG G:CYS41 4.8 20.0 1.0
CA G:GLY39 4.8 20.3 1.0
CB B:GLN72 5.0 15.8 1.0
CA G:GLN37 5.0 20.6 1.0

Iron binding site 8 out of 12 in 4e6k

Go back to Iron Binding Sites List in 4e6k
Iron binding site 8 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe101

b:18.4
occ:1.00
FE2 G:FES101 0.0 18.4 1.0
S1 G:FES101 2.2 19.7 1.0
S2 G:FES101 2.2 19.7 1.0
SG G:CYS4 2.3 19.6 1.0
SG G:CYS41 2.3 20.0 1.0
FE1 G:FES101 2.8 17.8 1.0
CB G:CYS4 3.2 16.1 1.0
CB G:CYS41 3.4 16.5 1.0
CA G:CYS4 3.5 17.5 1.0
N G:GLY35 3.8 20.6 1.0
CA G:GLY35 3.9 23.1 1.0
C G:CYS4 4.2 16.6 1.0
N G:CYS41 4.2 17.1 1.0
N G:LEU5 4.2 20.0 1.0
CB G:CYS6 4.4 18.7 1.0
N G:CYS6 4.4 18.3 1.0
CA G:CYS41 4.4 20.9 1.0
SG G:CYS6 4.5 20.8 1.0
SG G:CYS38 4.6 19.7 1.0
N G:GLY39 4.7 21.7 1.0
N G:CYS4 4.8 16.8 1.0
O G:VAL3 4.8 21.8 1.0
C G:GLY35 4.8 20.5 1.0
N G:LYS40 4.9 20.8 1.0
O B:HOH455 5.0 34.1 1.0
CA G:CYS6 5.0 15.8 1.0

Iron binding site 9 out of 12 in 4e6k

Go back to Iron Binding Sites List in 4e6k
Iron binding site 9 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe101

b:42.6
occ:1.00
FE1 H:FES101 0.0 42.6 1.0
S2 H:FES101 2.2 43.6 1.0
S1 H:FES101 2.2 46.6 1.0
SG H:CYS6 2.4 40.2 1.0
SG H:CYS38 2.5 41.5 1.0
FE2 H:FES101 2.9 45.0 1.0
CB H:CYS6 3.1 41.9 1.0
CB H:CYS38 3.5 48.1 1.0
N H:CYS38 3.5 57.0 1.0
N H:GLY39 3.8 49.9 1.0
CA H:CYS38 3.9 62.4 1.0
N H:CYS6 4.0 40.9 1.0
CA H:CYS6 4.2 42.8 1.0
C H:CYS38 4.3 48.9 1.0
CG C:GLN72 4.3 22.1 1.0
CB H:GLN37 4.5 57.4 1.0
SG H:CYS4 4.5 49.0 1.0
N H:LYS40 4.5 58.5 1.0
C H:GLN37 4.6 61.2 1.0
CA H:GLY39 4.9 56.6 1.0
SG H:CYS41 4.9 43.0 1.0
CB C:GLN72 4.9 19.1 1.0
CA H:GLN37 5.0 60.2 1.0

Iron binding site 10 out of 12 in 4e6k

Go back to Iron Binding Sites List in 4e6k
Iron binding site 10 out of 12 in the 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of 2.0 A Resolution Structure of Pseudomonas Aeruginosa Bacterioferritin (Bfrb) in Complex with Bacterioferritin Associated Ferredoxin (Bfd) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe101

b:45.0
occ:1.00
FE2 H:FES101 0.0 45.0 1.0
S1 H:FES101 2.2 46.6 1.0
S2 H:FES101 2.2 43.6 1.0
SG H:CYS4 2.4 49.0 1.0
SG H:CYS41 2.4 43.0 1.0
FE1 H:FES101 2.9 42.6 1.0
CB H:CYS4 3.2 47.2 1.0
CB H:CYS41 3.3 55.5 1.0
CA H:CYS4 3.6 46.8 1.0
N H:GLY35 3.7 66.8 1.0
CA H:GLY35 3.8 58.7 1.0
CB H:CYS6 4.2 41.9 1.0
C H:CYS4 4.3 47.5 1.0
N H:LEU5 4.3 52.0 1.0
N H:CYS41 4.4 55.6 1.0
CA H:CYS41 4.5 67.5 1.0
N H:CYS6 4.5 40.9 1.0
C H:GLY35 4.7 54.4 1.0
SG H:CYS6 4.7 40.2 1.0
N H:GLY39 4.7 49.9 1.0
O H:VAL3 4.8 44.5 1.0
N H:CYS4 4.9 41.3 1.0
C H:VAL34 4.9 70.6 1.0
SG H:CYS38 4.9 41.5 1.0
CA H:CYS6 5.0 42.8 1.0

Reference:

H.Yao, Y.Wang, S.Lovell, R.Kumar, A.M.Ruvinsky, K.P.Battaile, I.A.Vakser, M.Rivera. The Structure of the Bfrb-Bfd Complex Reveals Protein-Protein Interactions Enabling Iron Release From Bacterioferritin. J.Am.Chem.Soc. V. 134 13470 2012.
ISSN: ISSN 0002-7863
PubMed: 22812654
DOI: 10.1021/JA305180N
Page generated: Sun Dec 13 15:32:33 2020

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