Iron in PDB 8yay: Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene

All present enzymatic activity of Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene:
1.14.14.1; 1.6.2.4;

The structure of Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene, PDB code: 8yay was solved by S.Nagao, W.Kuwano, T.Tosha, K.Yamashita, J.K.Stanfield, C.Kasai, S.Ariyasu, O.Shoji, H.Sugimoto, M.Kubo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.91, 128.64, 149.45, 90, 90, 90
R / Rfree (%)	17.2 / 21.1

The binding sites of Iron atom in the Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene (pdb code 8yay). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene, PDB code: 8yay:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:32.3 occ:1.00 FE A:HEM501 0.0 32.3 1.0 ND A:HEM501 1.9 27.6 1.0 NA A:HEM501 2.0 32.2 1.0 O A:HOH670 2.1 36.6 0.6 NC A:HEM501 2.1 30.0 1.0 NB A:HEM501 2.1 30.9 1.0 SG A:CYS400 2.2 33.2 1.0 C4D A:HEM501 2.9 30.1 1.0 C1D A:HEM501 2.9 32.2 1.0 C1A A:HEM501 3.0 28.1 1.0 C4C A:HEM501 3.0 31.0 1.0 C4A A:HEM501 3.1 29.1 1.0 C1B A:HEM501 3.1 33.2 1.0 C4B A:HEM501 3.1 33.4 1.0 C1C A:HEM501 3.1 29.3 1.0 CB A:CYS400 3.3 31.4 1.0 CHD A:HEM501 3.4 33.8 1.0 CHA A:HEM501 3.4 31.4 1.0 CHB A:HEM501 3.5 34.4 1.0 CHC A:HEM501 3.5 31.6 1.0 O A:HOH635 3.6 34.3 0.7 CA A:CYS400 4.0 29.8 1.0 C3D A:HEM501 4.2 29.5 1.0 C2D A:HEM501 4.2 32.9 1.0 C2A A:HEM501 4.2 31.7 1.0 C3A A:HEM501 4.2 28.7 1.0 C3C A:HEM501 4.3 34.4 1.0 C2C A:HEM501 4.3 31.9 1.0 C2B A:HEM501 4.3 29.6 1.0 C3B A:HEM501 4.3 30.6 1.0 CE2 A:PHE87 4.4 34.5 0.6 C A:CYS400 4.7 34.1 1.0 O A:ALA264 4.8 38.8 1.0 N A:GLY402 4.9 31.8 1.0 N A:ILE401 5.0 34.8 1.0

Iron binding site 2 out of 2 in the Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Xfel Crystal Structure of the Oxidized Form of F393H P450BM3 with N- Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:32.5 occ:1.00 FE B:HEM501 0.0 32.5 1.0 ND B:HEM501 1.9 28.4 1.0 NA B:HEM501 2.0 32.5 1.0 O B:HOH687 2.0 32.4 0.4 NC B:HEM501 2.1 30.6 1.0 NB B:HEM501 2.1 30.2 1.0 SG B:CYS400 2.2 32.5 1.0 C4D B:HEM501 2.9 32.5 1.0 C1D B:HEM501 3.0 32.2 1.0 C1A B:HEM501 3.0 32.3 1.0 C4A B:HEM501 3.0 30.6 1.0 C4B B:HEM501 3.0 33.5 1.0 C1B B:HEM501 3.1 32.2 1.0 C4C B:HEM501 3.1 32.8 1.0 C1C B:HEM501 3.1 29.8 1.0 CB B:CYS400 3.2 30.7 1.0 CHA B:HEM501 3.4 33.0 1.0 CHD B:HEM501 3.4 33.5 1.0 CHB B:HEM501 3.5 31.4 1.0 CHC B:HEM501 3.5 32.2 1.0 O B:HOH620 3.5 32.0 0.7 CA B:CYS400 4.0 28.0 1.0 C3D B:HEM501 4.2 30.4 1.0 C2D B:HEM501 4.2 31.4 1.0 C3A B:HEM501 4.2 31.1 1.0 C2A B:HEM501 4.2 31.9 1.0 C3C B:HEM501 4.3 30.8 1.0 C2C B:HEM501 4.3 33.4 1.0 C2B B:HEM501 4.3 29.0 1.0 C3B B:HEM501 4.3 29.7 1.0 CE2 B:PHE87 4.4 31.7 0.7 C B:CYS400 4.7 31.9 1.0 O B:ALA264 4.8 36.7 1.0 CD2 B:HIS393 4.9 39.1 1.0 N B:GLY402 4.9 35.0 1.0 N B:ILE401 5.0 31.1 1.0

S.Nagao, W.Kuwano, T.Tosha, K.Yamashita, J.K.Stanfield, C.Kasai, S.Ariyasu, O.Shoji, H.Sugimoto, M.Kubo. Xfel Crystallography Reveals Dynamic Control of Non-Natural Substrate Binding in Cytochrome P450BM3 Catalytic Cycle To Be Published.