Iron in PDB 6gq8: Superoxide Reductase From Nanoarchaeum Equitans

The structure of Superoxide Reductase From Nanoarchaeum Equitans, PDB code: 6gq8 was solved by C.V.Romao, P.M.Matias, M.Teixeira, T.M.Bandeiras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.10 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.880, 82.010, 91.300, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24

The binding sites of Iron atom in the Superoxide Reductase From Nanoarchaeum Equitans (pdb code 6gq8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Superoxide Reductase From Nanoarchaeum Equitans, PDB code: 6gq8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Superoxide Reductase From Nanoarchaeum Equitans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Superoxide Reductase From Nanoarchaeum Equitans within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:41.2 occ:1.00 ND1 A:HIS100 2.2 46.3 1.0 NE2 A:HIS10 2.2 46.4 1.0 NE2 A:HIS35 2.2 48.1 1.0 NE2 A:HIS41 2.3 48.5 1.0 SG A:CYS97 2.5 36.5 1.0 CE1 A:HIS100 3.0 49.4 1.0 CD2 A:HIS10 3.1 46.2 1.0 CE1 A:HIS35 3.2 46.2 1.0 CE1 A:HIS41 3.3 50.8 1.0 CD2 A:HIS35 3.3 49.7 1.0 CD2 A:HIS41 3.3 47.0 1.0 CE1 A:HIS10 3.3 49.8 1.0 CG A:HIS100 3.4 46.8 1.0 CB A:CYS97 3.7 33.4 1.0 CB A:HIS100 3.8 43.7 1.0 NE2 A:HIS100 4.2 51.9 1.0 CG A:HIS10 4.3 44.6 1.0 ND1 A:HIS35 4.3 46.5 1.0 ND1 A:HIS10 4.4 48.6 1.0 ND1 A:HIS41 4.4 50.1 1.0 CD2 A:HIS100 4.4 50.9 1.0 CG A:HIS35 4.4 49.6 1.0 CG A:HIS41 4.4 47.3 1.0 N A:HIS100 4.5 37.7 1.0 CA A:HIS100 4.8 39.8 1.0 CB A:LEU99 4.9 39.4 1.0

Iron binding site 2 out of 4 in the Superoxide Reductase From Nanoarchaeum Equitans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Superoxide Reductase From Nanoarchaeum Equitans within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:49.6 occ:1.00 ND1 B:HIS100 2.2 58.6 1.0 NE2 B:HIS35 2.2 76.8 1.0 NE2 B:HIS41 2.2 53.2 1.0 NE2 B:HIS10 2.2 58.7 1.0 SG B:CYS97 2.4 40.1 1.0 CE1 B:HIS100 3.0 59.1 1.0 CD2 B:HIS10 3.1 56.7 1.0 CE1 B:HIS35 3.1 74.8 1.0 CD2 B:HIS41 3.2 50.6 1.0 CE1 B:HIS41 3.2 55.9 1.0 CD2 B:HIS35 3.3 79.1 1.0 CE1 B:HIS10 3.3 62.4 1.0 CG B:HIS100 3.3 53.4 1.0 CB B:CYS97 3.7 30.7 1.0 CB B:HIS100 3.7 42.0 1.0 NE2 B:HIS100 4.2 58.8 1.0 ND1 B:HIS35 4.3 75.0 1.0 CG B:HIS10 4.3 55.5 1.0 ND1 B:HIS41 4.3 55.1 1.0 CG B:HIS41 4.3 52.0 1.0 CD2 B:HIS100 4.3 59.6 1.0 ND1 B:HIS10 4.4 61.3 1.0 CG B:HIS35 4.4 73.8 1.0 N B:HIS100 4.4 37.9 1.0 CA B:HIS100 4.7 40.4 1.0 CB B:LEU99 4.9 38.9 1.0

Iron binding site 3 out of 4 in the Superoxide Reductase From Nanoarchaeum Equitans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Superoxide Reductase From Nanoarchaeum Equitans within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:48.0 occ:1.00 NE2 C:HIS35 2.1 71.8 1.0 ND1 C:HIS100 2.2 66.0 1.0 NE2 C:HIS41 2.3 59.7 1.0 NE2 C:HIS10 2.3 57.9 1.0 SG C:CYS97 2.4 40.5 1.0 O C:HOH327 2.6 51.5 1.0 CE1 C:HIS100 3.0 63.9 1.0 CE1 C:HIS35 3.1 65.3 1.0 CD2 C:HIS10 3.2 53.6 1.0 CD2 C:HIS35 3.2 67.2 1.0 CE1 C:HIS41 3.3 60.7 1.0 CD2 C:HIS41 3.3 61.6 1.0 CG C:HIS100 3.3 61.1 1.0 CE1 C:HIS10 3.4 59.5 1.0 CB C:CYS97 3.7 35.0 1.0 CB C:HIS100 3.8 51.1 1.0 NE2 C:HIS100 4.1 66.0 1.0 ND1 C:HIS35 4.2 63.3 1.0 CG C:HIS35 4.3 64.4 1.0 CD2 C:HIS100 4.3 66.2 1.0 CG C:HIS10 4.4 54.1 1.0 ND1 C:HIS41 4.4 61.1 1.0 N C:HIS100 4.4 41.5 1.0 CG C:HIS41 4.5 57.9 1.0 ND1 C:HIS10 4.5 56.9 1.0 CA C:HIS100 4.8 47.2 1.0 CB C:LEU99 5.0 43.2 1.0

Iron binding site 4 out of 4 in the Superoxide Reductase From Nanoarchaeum Equitans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Superoxide Reductase From Nanoarchaeum Equitans within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:46.8 occ:1.00 ND1 D:HIS100 2.2 69.5 1.0 NE2 D:HIS10 2.3 64.7 1.0 NE2 D:HIS41 2.3 54.4 1.0 NE2 D:HIS35 2.3 53.8 1.0 SG D:CYS97 2.4 39.4 1.0 CE1 D:HIS100 2.9 69.5 1.0 CD2 D:HIS10 3.2 61.7 1.0 CD2 D:HIS41 3.2 52.9 1.0 CG D:HIS100 3.2 62.4 1.0 CE1 D:HIS35 3.3 52.5 1.0 CD2 D:HIS35 3.3 55.2 1.0 CE1 D:HIS10 3.3 67.1 1.0 CE1 D:HIS41 3.3 57.6 1.0 CB D:HIS100 3.7 51.3 1.0 CB D:CYS97 3.7 34.3 1.0 NE2 D:HIS100 4.0 69.6 1.0 CD2 D:HIS100 4.1 67.3 1.0 CG D:HIS10 4.3 61.3 1.0 CG D:HIS41 4.4 53.5 1.0 N D:HIS100 4.4 43.9 1.0 ND1 D:HIS10 4.4 64.7 1.0 ND1 D:HIS35 4.4 52.5 1.0 ND1 D:HIS41 4.4 57.7 1.0 CG D:HIS35 4.4 54.2 1.0 CA D:HIS100 4.7 46.6 1.0 CB D:LEU99 4.9 46.8 1.0

C.V.Romao, P.M.Matias, C.M.Sousa, F.G.Pinho, A.F.Pinto, M.Teixeira, T.M.Bandeiras. Insights Into the Structures of Superoxide Reductases From the Symbionts Ignicoccus Hospitalis and Nanoarchaeum Equitans. Biochemistry V. 57 5271 2018.
ISSN: ISSN 1520-4995
PubMed: 29939726
DOI: 10.1021/ACS.BIOCHEM.8B00334