Iron in PDB 3cbd: Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3

All present enzymatic activity of Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3:
1.14.14.1;

The structure of Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3, PDB code: 3cbd was solved by Y.T.Meharenna, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.53 / 2.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.781, 127.346, 183.342, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 25.8

The binding sites of Iron atom in the Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3 (pdb code 3cbd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3, PDB code: 3cbd:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe460 b:57.6 occ:1.00 FE A:HEM460 0.0 57.6 1.0 NC A:HEM460 2.0 57.3 1.0 NA A:HEM460 2.0 57.6 1.0 ND A:HEM460 2.0 58.8 1.0 NB A:HEM460 2.0 58.6 1.0 SG A:CYS400 2.2 57.5 1.0 C4C A:HEM460 3.0 57.9 1.0 C1C A:HEM460 3.1 57.2 1.0 C4A A:HEM460 3.1 58.8 1.0 C1D A:HEM460 3.1 58.4 1.0 C1A A:HEM460 3.1 58.7 1.0 C4B A:HEM460 3.1 58.3 1.0 C1B A:HEM460 3.1 59.4 1.0 C4D A:HEM460 3.1 58.6 1.0 CB A:CYS400 3.4 56.9 1.0 CHD A:HEM460 3.4 59.1 1.0 CHC A:HEM460 3.5 57.5 1.0 CHB A:HEM460 3.5 60.4 1.0 CHA A:HEM460 3.5 57.6 1.0 CA A:CYS400 4.0 56.1 1.0 C3C A:HEM460 4.3 57.3 1.0 C2C A:HEM460 4.3 57.7 1.0 C3A A:HEM460 4.3 59.2 1.0 C3B A:HEM460 4.3 58.9 1.0 C2A A:HEM460 4.3 60.2 1.0 C2D A:HEM460 4.3 57.4 1.0 C2B A:HEM460 4.3 58.9 1.0 C3D A:HEM460 4.3 58.4 1.0 O A:ALA264 4.4 59.5 1.0 N A:GLY402 4.8 57.6 1.0 CE2 A:PHE87 4.8 63.7 1.0 C A:CYS400 4.8 55.3 1.0 N A:ILE401 4.9 55.9 1.0 CB A:ALA264 5.0 59.1 1.0

Iron binding site 2 out of 2 in the Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Directed Evolution of Cytochrome P450 BM3, to Octane Monoxygenase 139-3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe460 b:36.8 occ:1.00 FE B:HEM460 0.0 36.8 1.0 ND B:HEM460 2.0 38.5 1.0 NC B:HEM460 2.0 39.0 1.0 NB B:HEM460 2.0 39.4 1.0 NA B:HEM460 2.0 39.4 1.0 SG B:CYS400 2.2 37.4 1.0 C1D B:HEM460 3.0 38.2 1.0 C4C B:HEM460 3.0 39.1 1.0 C4B B:HEM460 3.0 39.0 1.0 C4D B:HEM460 3.0 39.0 1.0 C1C B:HEM460 3.1 37.3 1.0 C4A B:HEM460 3.1 41.1 1.0 C1B B:HEM460 3.1 40.7 1.0 C1A B:HEM460 3.1 39.1 1.0 CB B:CYS400 3.3 38.9 1.0 O B:HOH523 3.4 40.8 1.0 CHD B:HEM460 3.4 39.7 1.0 CHC B:HEM460 3.4 39.0 1.0 CHA B:HEM460 3.5 39.3 1.0 CHB B:HEM460 3.5 41.3 1.0 CA B:CYS400 4.0 39.4 1.0 C2D B:HEM460 4.2 38.6 1.0 C3D B:HEM460 4.3 39.4 1.0 C3C B:HEM460 4.3 38.6 1.0 C3B B:HEM460 4.3 40.0 1.0 C2C B:HEM460 4.3 38.0 1.0 C2B B:HEM460 4.3 41.1 1.0 C3A B:HEM460 4.3 41.1 1.0 C2A B:HEM460 4.3 40.3 1.0 O B:ALA264 4.4 44.3 1.0 CE2 B:PHE87 4.6 32.8 1.0 C B:CYS400 4.8 38.6 1.0 N B:ILE401 4.8 39.5 1.0 CB B:ALA264 4.9 40.3 1.0 N B:GLY402 5.0 41.7 1.0

R.Fasan, Y.T.Meharenna, C.D.Snow, T.L.Poulos, F.H.Arnold. Evolutionary History of A Specialized P450 Propane Monooxygenase. J.Mol.Biol. V. 383 1069 2008.
ISSN: ISSN 0022-2836
PubMed: 18619466
DOI: 10.1016/J.JMB.2008.06.060