Iron in PDB 8sqp: Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant)

Enzymatic activity of Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant)

All present enzymatic activity of Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant):
1.16.3.1;

Protein crystallography data

The structure of Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant), PDB code: 8sqp was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.08 / 2.05
Space group P 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 112.069, 112.069, 112.069, 90, 90, 90
R / Rfree (%) 19.6 / 21.5

Other elements in 8sqp:

The structure of Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant) also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant) (pdb code 8sqp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant), PDB code: 8sqp:

Iron binding site 1 out of 1 in 8sqp

Go back to Iron Binding Sites List in 8sqp
Iron binding site 1 out of 1 in the Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant)


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 Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe205

b:43.6
occ:0.50
 FE A:HEM205 0.0 43.6 0.5
NB A:HEM205 2.0 47.8 0.5
NA A:HEM205 2.1 46.9 0.5
NC A:HEM205 2.1 47.6 0.5
ND A:HEM205 2.1 46.8 0.5
SD A:MET52 2.3 47.5 1.0
C1C A:HEM205 3.1 48.2 0.5
C4B A:HEM205 3.1 48.3 0.5
C1A A:HEM205 3.1 53.6 0.5
CE A:MET52 3.1 51.6 1.0
C1B A:HEM205 3.1 48.1 0.5
C4A A:HEM205 3.1 48.8 0.5
C4D A:HEM205 3.1 53.5 0.5
C1D A:HEM205 3.1 48.7 0.5
C4C A:HEM205 3.1 46.5 0.5
CHC A:HEM205 3.4 48.7 0.5
CG A:MET52 3.4 48.6 1.0
CHA A:HEM205 3.4 52.3 0.5
CHB A:HEM205 3.5 48.1 0.5
CHD A:HEM205 3.5 48.0 0.5
CB A:MET52 4.2 44.4 1.0
C2C A:HEM205 4.3 48.0 0.5
C2A A:HEM205 4.3 55.8 0.5
C3A A:HEM205 4.3 51.8 0.5
C3B A:HEM205 4.3 46.8 0.5
C2B A:HEM205 4.3 49.4 0.5
C3D A:HEM205 4.3 55.8 0.5
C3C A:HEM205 4.3 49.8 0.5
C2D A:HEM205 4.3 51.9 0.5

Reference:

S.Lovell, L.Liu, K.P.Battaile. Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo, F16L Mutant) To Be Published.
Page generated: Sat Aug 10 18:03:04 2024

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