Iron in PDB 8hoq: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr, PDB code: 8hoq was solved by Y.Jiang, S.Dong, Y.Feng, Z.Cong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.72 / 1.94
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.639, 147.949, 64.725, 90, 100.16, 90
R / Rfree (%)	17.8 / 20

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr (pdb code 8hoq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr, PDB code: 8hoq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr


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 the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:23.5 occ:1.00 FE A:HEM501 0.0 23.5 1.0 ND A:HEM501 2.0 20.8 1.0 NA A:HEM501 2.0 22.8 1.0 NC A:HEM501 2.1 22.8 1.0 NB A:HEM501 2.1 21.5 1.0 SG A:CYS400 2.5 24.5 1.0 O C:HOH101 2.5 31.0 1.0 C1D A:HEM501 3.1 23.3 1.0 C4C A:HEM501 3.1 26.3 1.0 C4D A:HEM501 3.1 21.4 1.0 C1B A:HEM501 3.1 22.4 1.0 C4A A:HEM501 3.1 26.9 1.0 C1A A:HEM501 3.1 24.0 1.0 C4B A:HEM501 3.1 22.0 1.0 C1C A:HEM501 3.1 25.6 1.0 CB A:CYS400 3.4 21.7 1.0 CHD A:HEM501 3.4 25.7 1.0 CHB A:HEM501 3.4 21.8 1.0 CHA A:HEM501 3.4 22.0 1.0 CHC A:HEM501 3.5 22.5 1.0 CA A:CYS400 4.1 23.8 1.0 O A:ALA264 4.2 36.7 1.0 C3D A:HEM501 4.3 20.4 1.0 C2D A:HEM501 4.3 23.2 1.0 C3A A:HEM501 4.3 23.0 1.0 C3C A:HEM501 4.3 21.9 1.0 C2B A:HEM501 4.3 22.4 1.0 C2A A:HEM501 4.3 22.0 1.0 C3B A:HEM501 4.3 22.1 1.0 C2C A:HEM501 4.3 26.5 1.0 CB A:ALA264 4.6 33.5 1.0 N A:GLY402 4.8 24.3 1.0 N34 C:I7X1 4.8 40.1 1.0 C A:ALA264 4.9 33.5 1.0 C A:CYS400 4.9 23.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:22.8 occ:1.00 FE B:HEM501 0.0 22.8 1.0 NB B:HEM501 2.0 21.2 1.0 NC B:HEM501 2.1 23.8 1.0 ND B:HEM501 2.1 19.8 1.0 NA B:HEM501 2.1 24.9 1.0 SG B:CYS400 2.4 23.9 1.0 O D:HOH101 2.5 32.4 1.0 C4B B:HEM501 3.0 22.9 1.0 C1B B:HEM501 3.0 23.0 1.0 C1C B:HEM501 3.1 24.8 1.0 C1D B:HEM501 3.1 22.4 1.0 C4A B:HEM501 3.1 23.5 1.0 C4D B:HEM501 3.1 23.3 1.0 C4C B:HEM501 3.1 24.1 1.0 C1A B:HEM501 3.1 24.6 1.0 CB B:CYS400 3.4 22.1 1.0 CHC B:HEM501 3.4 21.5 1.0 CHB B:HEM501 3.4 22.8 1.0 CHD B:HEM501 3.4 23.6 1.0 CHA B:HEM501 3.5 22.9 1.0 CA B:CYS400 4.1 24.7 1.0 O B:ALA264 4.2 32.3 1.0 C3B B:HEM501 4.3 25.1 1.0 C2B B:HEM501 4.3 25.2 1.0 C2C B:HEM501 4.3 25.9 1.0 C3D B:HEM501 4.3 23.2 1.0 C2D B:HEM501 4.3 25.3 1.0 C3A B:HEM501 4.3 24.9 1.0 C3C B:HEM501 4.3 20.6 1.0 C2A B:HEM501 4.3 25.6 1.0 CB B:ALA264 4.6 32.1 1.0 N34 D:I7X1 4.6 38.4 1.0 C B:ALA264 4.8 30.7 1.0 N B:GLY402 4.9 23.5 1.0 C B:CYS400 4.9 25.1 1.0 C33 D:I7X1 4.9 35.9 1.0

Y.Jiang, S.Dong, Y.Feng, Z.Cong. Crystal Structure of the P450 BM3 Heme Domain Mutant F87A in Complex with Im-C6-Phe(4CF3)-Tyr To Be Published.