Iron in PDB 4brj: Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K

The structure of Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K, PDB code: 4brj was solved by C.V.Romao, P.M.Matias, F.G.Pinho, C.M.Sousa, A.R.Barradas, A.F.Pinto, M.Teixeira, T.M.Bandeiras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.136 / 2.50
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	108.857, 108.857, 61.694, 90.00, 90.00, 120.00
R / Rfree (%)	17.42 / 24.11

The binding sites of Iron atom in the Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K (pdb code 4brj). 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 Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K, PDB code: 4brj:

Iron binding site 1 out of 1 in the Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Superoxide Reductase (Neelaredoxin) From Ignicoccus Hospitalis T24K within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1125 b:61.1 occ:1.00 NE2 A:HIS50 2.0 80.0 1.0 NE2 A:HIS25 2.1 76.6 1.0 ND1 A:HIS112 2.3 80.9 1.0 NE2 A:HIS56 2.4 74.2 1.0 SG A:CYS109 2.6 64.1 1.0 OE2 A:GLU23 2.8 0.5 1.0 CE1 A:HIS50 3.0 73.7 1.0 CE1 A:HIS25 3.0 78.3 1.0 CD2 A:HIS50 3.1 75.7 1.0 CD2 A:HIS25 3.2 55.9 1.0 CE1 A:HIS112 3.2 80.3 1.0 CG A:HIS112 3.2 76.6 1.0 CE1 A:HIS56 3.2 67.1 1.0 CD2 A:HIS56 3.4 69.0 1.0 CB A:HIS112 3.6 59.8 1.0 CB A:CYS109 3.8 56.3 1.0 CD A:GLU23 4.0 0.9 1.0 ND1 A:HIS50 4.1 68.4 1.0 ND1 A:HIS25 4.2 78.5 1.0 CG A:HIS50 4.2 75.2 1.0 CG A:HIS25 4.3 66.0 1.0 NE2 A:HIS112 4.3 79.7 1.0 CD2 A:HIS112 4.3 78.3 1.0 ND1 A:HIS56 4.4 71.1 1.0 CG A:HIS56 4.5 73.1 1.0 CG A:GLU23 4.6 0.3 1.0 N A:HIS112 4.6 63.1 1.0 CA A:HIS112 4.7 63.7 1.0

C.V.Romao, P.M.Matias, F.G.Pinho, C.M.Sousa, A.R.Barradas, A.F.Pinto, M.Teixeira, T.M.Bandeiras. Structure of A Natural Sor Mutant To Be Published.