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Iron in PDB 9bts: Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii

Enzymatic activity of Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii

All present enzymatic activity of Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii:
1.16.3.1;

Protein crystallography data

The structure of Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii, PDB code: 9bts was solved by S.Lovell, L.Liu, K.P.Battaile, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.72 / 1.85
Space group P 2 3
Cell size a, b, c (Å), α, β, γ (°) 173.028, 173.028, 173.028, 90, 90, 90
R / Rfree (%) 16.6 / 19.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii (pdb code 9bts). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii, PDB code: 9bts:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 9bts

Go back to Iron Binding Sites List in 9bts
Iron binding site 1 out of 4 in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii


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 the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe203

b:52.9
occ:0.56
 FE A:HEM203 0.0 52.9 0.6
NC A:HEM203 2.0 31.4 0.6
NB A:HEM203 2.0 31.1 0.6
NA A:HEM203 2.1 27.8 0.6
ND A:HEM203 2.1 24.8 0.6
SD B:MET52 2.4 26.5 0.6
SD A:MET52 2.4 24.4 0.6
C1C A:HEM203 3.0 23.9 0.6
C4B A:HEM203 3.0 31.3 0.6
C1B A:HEM203 3.1 27.8 0.6
C4C A:HEM203 3.1 26.8 0.6
C4A A:HEM203 3.1 24.6 0.6
C1A A:HEM203 3.1 26.8 0.6
C4D A:HEM203 3.1 23.9 0.6
C1D A:HEM203 3.1 28.9 0.6
CE B:MET52 3.2 27.6 0.6
CE A:MET52 3.2 27.8 0.6
CHC A:HEM203 3.3 25.9 0.6
CG B:MET52 3.4 28.8 0.6
CHB A:HEM203 3.4 30.3 0.6
CHA A:HEM203 3.4 29.5 0.6
CHD A:HEM203 3.5 29.6 0.6
CG A:MET52 3.5 25.7 0.6
CB b:ALA52 4.1 28.1 0.4
CB B:MET52 4.1 25.8 0.6
CB A:MET52 4.2 30.3 0.6
C3B A:HEM203 4.2 27.6 0.6
C2C A:HEM203 4.3 28.9 0.6
C2B A:HEM203 4.3 24.0 0.6
C3C A:HEM203 4.3 20.6 0.6
C3A A:HEM203 4.3 21.6 0.6
C2A A:HEM203 4.3 23.5 0.6
C3D A:HEM203 4.3 23.4 0.6
C2D A:HEM203 4.4 30.5 0.6
CB a:ALA52 4.4 29.0 0.4
OE1 a:GLN49 4.5 49.0 0.4
SD b:MET48 4.6 47.1 0.4
CD b:ARG22 4.6 28.3 0.4
CD1 B:ILE49 4.9 36.8 0.6
SD a:MET48 4.9 41.4 0.4
CD a:ARG22 4.9 33.2 0.4

Iron binding site 2 out of 4 in 9bts

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Iron binding site 2 out of 4 in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii


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 the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:29.2
occ:0.56
 FE C:HEM201 0.0 29.2 0.6
NB C:HEM201 1.9 32.6 0.6
NC C:HEM201 2.0 33.0 0.6
NA C:HEM201 2.0 32.4 0.6
ND C:HEM201 2.0 32.7 0.6
SD C:MET52 2.3 25.3 0.6
SD D:MET52 2.4 24.8 0.6
C4B C:HEM201 2.9 31.0 0.6
C1B C:HEM201 2.9 24.8 0.6
C1C C:HEM201 3.0 32.1 0.6
C4A C:HEM201 3.0 28.1 0.6
C4C C:HEM201 3.1 31.0 0.6
C1D C:HEM201 3.1 27.5 0.6
C4D C:HEM201 3.1 30.6 0.6
C1A C:HEM201 3.1 35.1 0.6
CE D:MET52 3.3 29.7 0.6
CHC C:HEM201 3.3 32.5 0.6
CE C:MET52 3.4 28.4 0.6
CHB C:HEM201 3.4 30.4 0.6
CG C:MET52 3.5 26.4 0.6
CG D:MET52 3.5 33.8 0.6
CHA C:HEM201 3.5 29.6 0.6
CHD C:HEM201 3.5 35.0 0.6
NE2 c:GLN49 4.1 47.1 0.4
C2B C:HEM201 4.1 18.6 0.6
C3B C:HEM201 4.1 28.3 0.6
CB c:ALA52 4.1 29.5 0.4
CB C:MET52 4.2 30.4 0.6
CB D:MET52 4.2 27.5 0.6
C2C C:HEM201 4.2 23.6 0.6
C3C C:HEM201 4.2 29.5 0.6
C3A C:HEM201 4.3 34.1 0.6
C2D C:HEM201 4.3 30.4 0.6
C2A C:HEM201 4.3 33.5 0.6
C3D C:HEM201 4.3 31.0 0.6
CB d:ALA52 4.4 27.0 0.4
SD d:MET48 4.6 44.2 0.4
NE2 d:GLN49 4.7 51.7 0.4
CD c:ARG22 4.7 28.3 0.4
CD d:ARG22 4.8 29.5 0.4
SD c:MET48 4.9 48.1 0.4

Iron binding site 3 out of 4 in 9bts

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Iron binding site 3 out of 4 in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii


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 the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe202

b:34.4
occ:0.56
 FE F:HEM202 0.0 34.4 0.6
NC F:HEM202 2.0 33.8 0.6
NB F:HEM202 2.0 28.5 0.6
NA F:HEM202 2.1 27.1 0.6
ND F:HEM202 2.1 27.2 0.6
SD F:MET52 2.3 26.2 0.6
SD E:MET52 2.3 27.3 0.6
C1C F:HEM202 3.0 27.3 0.6
C4C F:HEM202 3.0 27.5 0.6
C1B F:HEM202 3.0 26.1 0.6
C4B F:HEM202 3.0 29.6 0.6
C1A F:HEM202 3.1 30.3 0.6
C4D F:HEM202 3.1 27.6 0.6
C4A F:HEM202 3.1 26.8 0.6
C1D F:HEM202 3.1 24.8 0.6
CE E:MET52 3.3 28.9 0.6
CE F:MET52 3.3 31.0 0.6
CHC F:HEM202 3.4 26.6 0.6
CHD F:HEM202 3.4 29.9 0.6
CHB F:HEM202 3.4 31.1 0.6
CHA F:HEM202 3.4 29.4 0.6
CG E:MET52 3.4 26.3 0.6
CG F:MET52 3.5 27.2 0.6
CB e:ALA52 4.1 29.6 0.4
CB E:MET52 4.2 26.4 0.6
C2C F:HEM202 4.2 25.2 0.6
CB F:MET52 4.2 28.8 0.6
C3C F:HEM202 4.2 24.9 0.6
C2B F:HEM202 4.2 18.9 0.6
C3B F:HEM202 4.3 27.5 0.6
C3A F:HEM202 4.3 27.8 0.6
C2A F:HEM202 4.3 31.3 0.6
C3D F:HEM202 4.3 30.5 0.6
C2D F:HEM202 4.3 27.8 0.6
NE2 e:GLN49 4.4 50.2 0.4
CB f:ALA52 4.5 28.5 0.4
NE2 f:GLN49 4.5 50.9 0.4
CD e:ARG22 4.6 30.9 0.4
SD e:MET48 4.7 47.0 0.4
SD f:MET48 4.8 43.8 0.4
CD f:ARG22 4.9 31.7 0.4

Iron binding site 4 out of 4 in 9bts

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Iron binding site 4 out of 4 in the Crystal Structure of the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii


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 the Bacterioferritin (Bfr) and Ferritin (Ftn) Heterooligomer Complex From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe202

b:32.9
occ:0.56
 FE H:HEM202 0.0 32.9 0.6
NC H:HEM202 2.0 28.1 0.6
NB H:HEM202 2.0 26.5 0.6
NA H:HEM202 2.0 32.4 0.6
ND H:HEM202 2.0 31.7 0.6
SD G:MET52 2.3 27.9 0.6
SD H:MET52 2.3 25.6 0.6
C1C H:HEM202 3.0 28.6 0.6
C4B H:HEM202 3.0 28.9 0.6
C1B H:HEM202 3.0 28.7 0.6
C4D H:HEM202 3.1 31.1 0.6
C1A H:HEM202 3.1 33.7 0.6
C4C H:HEM202 3.1 25.4 0.6
C4A H:HEM202 3.1 29.0 0.6
C1D H:HEM202 3.1 26.4 0.6
CE H:MET52 3.3 32.8 0.6
CE G:MET52 3.3 33.3 0.6
CHC H:HEM202 3.3 29.3 0.6
CHA H:HEM202 3.4 33.8 0.6
CHB H:HEM202 3.4 28.1 0.6
CHD H:HEM202 3.5 28.2 0.6
CG H:MET52 3.5 28.1 0.6
CG G:MET52 3.5 26.6 0.6
CB h:ALA52 4.0 30.6 0.4
CB H:MET52 4.2 28.8 0.6
NE2 h:GLN49 4.2 49.4 0.4
C3B H:HEM202 4.2 24.4 0.6
CB G:MET52 4.2 27.2 0.6
C2B H:HEM202 4.2 27.2 0.6
C2C H:HEM202 4.2 27.3 0.6
C3C H:HEM202 4.2 20.9 0.6
C2A H:HEM202 4.3 33.0 0.6
C3A H:HEM202 4.3 29.1 0.6
C3D H:HEM202 4.3 30.2 0.6
C2D H:HEM202 4.3 32.4 0.6
CB g:ALA52 4.4 26.6 0.4
NE2 g:GLN49 4.5 50.6 0.4
CD h:ARG22 4.7 25.5 0.4
SD g:MET48 4.8 45.2 0.4
SD h:MET48 4.8 49.7 0.4

Reference:

H.Yao, S.Alli, L.Liu, A.Soldano, A.Cooper, L.Fontenot, D.Verdin, K.P.Battaile, S.Lovell, M.Rivera. The Crystal Structure of Acinetobacter Baumannii Bacterioferritin Reveals A Heteropolymer of Bacterioferritin and Ferritin Subunits Sci Rep V. 14 18242 2024.
ISSN: ESSN 2045-2322
DOI: 10.1038/S41598-024-69156-2
Page generated: Sat Sep 28 21:55:02 2024

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