Iron in PDB 8yb1: Xfel Crystal Structure of the Reduced Form of F87A/F393H P450BM3 with N-Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene

All present enzymatic activity of Xfel Crystal Structure of the Reduced Form of F87A/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 Reduced Form of F87A/F393H P450BM3 with N-Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene, PDB code: 8yb1 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 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.86, 128.49, 149.51, 90, 90, 90
R / Rfree (%)	18.4 / 21.4

The binding sites of Iron atom in the Xfel Crystal Structure of the Reduced Form of F87A/F393H P450BM3 with N-Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene (pdb code 8yb1). 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 Reduced Form of F87A/F393H P450BM3 with N-Enanthyl-L-Prolyl-L-Phenylalanine in Complex with Styrene, PDB code: 8yb1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Xfel Crystal Structure of the Reduced Form of F87A/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 Reduced Form of F87A/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:30.0 occ:1.00 FE A:HEM501 0.0 30.0 1.0 ND A:HEM501 1.9 28.6 1.0 NA A:HEM501 2.0 32.4 1.0 NB A:HEM501 2.1 29.0 1.0 NC A:HEM501 2.1 30.3 1.0 SG A:CYS400 2.4 31.9 1.0 C1D A:HEM501 2.9 31.5 1.0 C4D A:HEM501 2.9 30.2 1.0 C1A A:HEM501 3.0 27.6 1.0 C4C A:HEM501 3.1 32.9 1.0 C4B A:HEM501 3.1 31.4 1.0 C1B A:HEM501 3.1 35.5 1.0 C4A A:HEM501 3.1 31.1 1.0 C1C A:HEM501 3.1 28.7 1.0 CB A:CYS400 3.3 30.2 1.0 CHD A:HEM501 3.4 33.1 1.0 CHA A:HEM501 3.4 29.7 1.0 O A:HOH641 3.4 36.6 1.0 CHB A:HEM501 3.5 31.7 1.0 CHC A:HEM501 3.5 31.0 1.0 CA A:CYS400 4.0 32.6 1.0 CAE A:SYN503 4.1 37.0 0.4 C2D A:HEM501 4.2 34.5 1.0 C3D A:HEM501 4.2 31.9 1.0 C2A A:HEM501 4.3 30.7 1.0 C3A A:HEM501 4.3 31.1 1.0 CAA A:SYN503 4.3 37.2 0.4 C3C A:HEM501 4.3 35.9 1.0 C2B A:HEM501 4.3 31.7 1.0 C3B A:HEM501 4.3 29.0 1.0 C2C A:HEM501 4.3 33.8 1.0 O A:HOH614 4.4 40.3 1.0 CAG A:SYN503 4.7 40.4 0.4 C A:CYS400 4.8 35.7 1.0 N A:GLY402 4.8 29.2 1.0 O A:ALA264 4.9 35.7 1.0 N A:ILE401 4.9 33.3 1.0

Iron binding site 2 out of 2 in the Xfel Crystal Structure of the Reduced Form of F87A/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 Reduced Form of F87A/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:30.4 occ:1.00 FE B:HEM501 0.0 30.4 1.0 ND B:HEM501 1.9 27.3 1.0 NA B:HEM501 2.0 31.1 1.0 NC B:HEM501 2.1 30.4 1.0 NB B:HEM501 2.1 30.8 1.0 SG B:CYS400 2.4 31.2 1.0 C4D B:HEM501 2.9 31.6 1.0 C1D B:HEM501 3.0 31.4 1.0 C1A B:HEM501 3.0 31.1 1.0 C4B B:HEM501 3.1 33.2 1.0 C1B B:HEM501 3.1 34.2 1.0 C4A B:HEM501 3.1 32.1 1.0 C4C B:HEM501 3.1 33.2 1.0 C1C B:HEM501 3.1 31.3 1.0 CB B:CYS400 3.3 30.2 1.0 CHA B:HEM501 3.4 30.5 1.0 CHD B:HEM501 3.4 31.1 1.0 CHB B:HEM501 3.5 29.1 1.0 O B:HOH687 3.5 35.8 1.0 CHC B:HEM501 3.5 30.9 1.0 CA B:CYS400 4.0 29.9 1.0 CAE B:SYN503 4.1 35.0 0.5 O B:HOH601 4.1 43.7 1.0 C3D B:HEM501 4.2 32.4 1.0 C2D B:HEM501 4.2 32.5 1.0 C2A B:HEM501 4.2 31.7 1.0 C3A B:HEM501 4.3 30.7 1.0 C2B B:HEM501 4.3 31.9 1.0 C3C B:HEM501 4.3 30.3 1.0 C3B B:HEM501 4.3 27.5 1.0 C2C B:HEM501 4.3 34.2 1.0 CAA B:SYN503 4.5 36.1 0.4 CAG B:SYN503 4.7 38.1 0.5 C B:CYS400 4.8 31.9 1.0 O B:ALA264 4.8 34.9 1.0 N B:ILE401 4.9 29.7 1.0 N B:GLY402 4.9 33.1 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.