Iron in PDB 1oxa: Cytochrome P450 (Donor:O2 Oxidoreductase)

The structure of Cytochrome P450 (Donor:O2 Oxidoreductase), PDB code: 1oxa was solved by J.R.Cupp-Vickery, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.160, 79.670, 99.480, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / n/a

The binding sites of Iron atom in the Cytochrome P450 (Donor:O2 Oxidoreductase) (pdb code 1oxa). 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 Cytochrome P450 (Donor:O2 Oxidoreductase), PDB code: 1oxa:

Iron binding site 1 out of 1 in the Cytochrome P450 (Donor:O2 Oxidoreductase)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 (Donor:O2 Oxidoreductase) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe410 b:10.8 occ:1.00 FE A:HEM410 0.0 10.8 1.0 NB A:HEM410 1.9 11.2 1.0 ND A:HEM410 2.0 9.0 1.0 NA A:HEM410 2.0 8.6 1.0 NC A:HEM410 2.0 12.9 1.0 SG A:CYS351 2.2 16.5 1.0 C4B A:HEM410 2.9 9.6 1.0 C1B A:HEM410 3.0 10.2 1.0 C1C A:HEM410 3.0 8.1 1.0 C4A A:HEM410 3.0 7.2 1.0 C4D A:HEM410 3.0 9.9 1.0 C1D A:HEM410 3.0 8.4 1.0 C1A A:HEM410 3.1 8.5 1.0 C4C A:HEM410 3.1 9.0 1.0 CHC A:HEM410 3.3 8.1 1.0 CHB A:HEM410 3.4 8.3 1.0 CB A:CYS351 3.4 13.5 1.0 CHA A:HEM410 3.4 6.5 1.0 CHD A:HEM410 3.5 8.6 1.0 O A:HOH519 3.8 19.2 1.0 CA A:CYS351 4.0 11.1 1.0 C3B A:HEM410 4.2 11.5 1.0 C2B A:HEM410 4.2 8.9 1.0 C3A A:HEM410 4.3 8.3 1.0 C3D A:HEM410 4.3 8.2 1.0 C2D A:HEM410 4.3 7.1 1.0 C2A A:HEM410 4.3 7.7 1.0 C2C A:HEM410 4.3 10.9 1.0 C3C A:HEM410 4.3 12.3 1.0 N A:GLY353 4.6 12.1 1.0 N A:MET352 4.7 8.9 1.0 C A:CYS351 4.7 8.9 1.0 C23 A:DEB420 4.8 14.6 1.0 C6 A:DEB420 4.8 19.3 1.0

J.R.Cupp-Vickery, T.L.Poulos. Structure of Cytochrome P450ERYF Involved in Erythromycin Biosynthesis. Nat.Struct.Biol. V. 2 144 1995.
ISSN: ISSN 1072-8368
PubMed: 7749919
DOI: 10.1038/NSB0295-144