Iron in PDB 1fah: Structure of Cytochrome P450

All present enzymatic activity of Structure of Cytochrome P450:
1.14.14.1;

The structure of Structure of Cytochrome P450, PDB code: 1fah was solved by H.Y.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.500, 154.000, 62.400, 90.00, 95.00, 90.00
R / Rfree (%)	17.2 / n/a

The binding sites of Iron atom in the Structure of Cytochrome P450 (pdb code 1fah). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Cytochrome P450, PDB code: 1fah:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Cytochrome P450


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome P450 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe472 b:10.1 occ:1.00 FE A:HEM472 0.0 10.1 1.0 O A:HOH473 1.9 5.6 1.0 NA A:HEM472 2.0 7.6 1.0 NC A:HEM472 2.0 5.6 1.0 NB A:HEM472 2.0 12.2 1.0 ND A:HEM472 2.0 16.9 1.0 SG A:CYS400 2.0 5.3 1.0 C4C A:HEM472 3.0 8.4 1.0 C1C A:HEM472 3.0 4.0 1.0 C4A A:HEM472 3.0 11.8 1.0 C1A A:HEM472 3.0 14.4 1.0 C4B A:HEM472 3.1 13.1 1.0 C1B A:HEM472 3.1 6.2 1.0 C1D A:HEM472 3.1 14.9 1.0 C4D A:HEM472 3.1 14.2 1.0 CB A:CYS400 3.2 12.0 1.0 CHB A:HEM472 3.4 10.7 1.0 CHC A:HEM472 3.4 10.6 1.0 CHD A:HEM472 3.4 11.5 1.0 CHA A:HEM472 3.5 14.8 1.0 CA A:CYS400 4.0 9.2 1.0 C3C A:HEM472 4.3 7.7 1.0 C2C A:HEM472 4.3 3.7 1.0 C2A A:HEM472 4.3 9.7 1.0 C3A A:HEM472 4.3 4.6 1.0 C3B A:HEM472 4.3 11.8 1.0 C2B A:HEM472 4.3 9.4 1.0 C2D A:HEM472 4.3 10.3 1.0 C3D A:HEM472 4.4 9.2 1.0 O A:ALA264 4.4 14.0 1.0 O A:HOH619 4.6 34.4 1.0 C A:CYS400 4.8 10.7 1.0 N A:GLY402 4.9 4.1 1.0

Iron binding site 2 out of 2 in the Structure of Cytochrome P450


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Cytochrome P450 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe472 b:12.4 occ:1.00 FE B:HEM472 0.0 12.4 1.0 NC B:HEM472 2.0 11.0 1.0 NA B:HEM472 2.0 14.4 1.0 O B:HOH473 2.0 5.9 1.0 ND B:HEM472 2.0 20.4 1.0 NB B:HEM472 2.0 15.2 1.0 SG B:CYS400 2.1 8.4 1.0 C4C B:HEM472 3.0 14.8 1.0 C1C B:HEM472 3.0 15.5 1.0 C1A B:HEM472 3.0 15.8 1.0 C4A B:HEM472 3.0 13.2 1.0 C4B B:HEM472 3.1 15.6 1.0 C1D B:HEM472 3.1 17.2 1.0 C4D B:HEM472 3.1 11.9 1.0 C1B B:HEM472 3.1 14.7 1.0 CB B:CYS400 3.2 15.8 1.0 CHD B:HEM472 3.4 17.2 1.0 CHC B:HEM472 3.4 13.2 1.0 CHA B:HEM472 3.4 14.5 1.0 CHB B:HEM472 3.4 10.9 1.0 CA B:CYS400 3.9 12.3 1.0 O B:HOH549 4.2 39.1 1.0 C2C B:HEM472 4.3 13.0 1.0 C3C B:HEM472 4.3 14.0 1.0 C2A B:HEM472 4.3 14.2 1.0 C3D B:HEM472 4.3 15.8 1.0 C3A B:HEM472 4.3 14.0 1.0 C2D B:HEM472 4.3 16.2 1.0 C3B B:HEM472 4.3 17.4 1.0 C2B B:HEM472 4.3 18.0 1.0 O B:ALA264 4.4 15.6 1.0 C B:CYS400 4.7 12.1 1.0 N B:ILE401 4.9 13.7 1.0 N B:GLY402 4.9 14.3 1.0

H.Yeom, S.G.Sligar, H.Li, T.L.Poulos, A.J.Fulco. The Role of THR268 in Oxygen Activation of Cytochrome P450BM-3. Biochemistry V. 34 14733 1995.
ISSN: ISSN 0006-2960
PubMed: 7578081
DOI: 10.1021/BI00045A014