Iron in PDB 8sqq: Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo Cubic Form 2, F16L Mutant)

Enzymatic activity of Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo Cubic Form 2, F16L Mutant)

Protein crystallography data

Other elements in 8sqq:

Iron Binding Sites:

Iron binding site 1 out of 1 in 8sqq

Iron Binding Sites List in 8sqq

Iron binding site 1 out of 1 in the Crystal Structure of Bacterioferritin (Bfr) From Brucella Abortus (Apo Cubic Form 2, 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 Cubic Form 2, F16L Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe205 b:38.7 occ:0.50 FE A:HEM205 0.0 38.7 0.5 NB A:HEM205 1.9 44.4 0.5 NC A:HEM205 2.0 44.3 0.5 NA A:HEM205 2.1 45.9 0.5 ND A:HEM205 2.1 45.9 0.5 SD A:MET52 2.3 43.0 1.0 C4B A:HEM205 3.0 42.6 0.5 C1B A:HEM205 3.0 44.2 0.5 C1C A:HEM205 3.0 42.5 0.5 C4C A:HEM205 3.1 44.3 0.5 C4A A:HEM205 3.1 46.8 0.5 C1A A:HEM205 3.1 45.7 0.5 C1D A:HEM205 3.1 46.0 0.5 C4D A:HEM205 3.2 45.8 0.5 CHC A:HEM205 3.3 41.8 0.5 CE A:MET52 3.4 44.6 1.0 CG A:MET52 3.4 44.1 1.0 CHB A:HEM205 3.4 44.6 0.5 CHD A:HEM205 3.5 44.5 0.5 CHA A:HEM205 3.5 46.4 0.5 CB A:MET52 4.1 42.0 1.0 C3B A:HEM205 4.2 42.8 0.5 C2B A:HEM205 4.2 43.9 0.5 C2C A:HEM205 4.2 42.7 0.5 C3C A:HEM205 4.3 43.7 0.5 C3A A:HEM205 4.3 46.1 0.5 C2A A:HEM205 4.3 49.4 0.5 C2D A:HEM205 4.4 51.3 0.5 C3D A:HEM205 4.4 49.4 0.5

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