Iron in PDB 6l1b: Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine

All present enzymatic activity of Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine, PDB code: 6l1b was solved by O.Shoji, K.Yonemura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 1.74
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.854, 148.303, 63.691, 90.00, 98.61, 90.00
R / Rfree (%)	17.2 / 20.3

The binding sites of Iron atom in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine (pdb code 6l1b). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine, PDB code: 6l1b:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine


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 P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.4 occ:0.39 FE A:HEM501 0.0 15.4 0.4 FE A:HEM501 0.0 13.0 0.6 ND A:HEM501 1.9 14.3 0.4 ND A:HEM501 2.0 12.7 0.6 NA A:HEM501 2.0 11.4 0.6 NA A:HEM501 2.0 15.5 0.4 NB A:HEM501 2.1 12.6 0.6 NC A:HEM501 2.1 12.1 0.6 NC A:HEM501 2.1 15.0 0.4 NB A:HEM501 2.1 14.8 0.4 SG A:CYS400 2.3 15.0 1.0 S A:DMS502 2.3 22.8 1.0 C1D A:HEM501 2.9 14.7 0.4 C4D A:HEM501 2.9 14.7 0.4 C4D A:HEM501 3.0 12.2 0.6 C1D A:HEM501 3.0 12.1 0.6 C1A A:HEM501 3.0 11.8 0.6 C4A A:HEM501 3.0 12.1 0.6 C4B A:HEM501 3.0 13.1 0.6 C4C A:HEM501 3.0 15.0 0.4 C4B A:HEM501 3.0 15.8 0.4 C1A A:HEM501 3.0 15.1 0.4 C1B A:HEM501 3.0 12.5 0.6 C4C A:HEM501 3.0 13.0 0.6 C1C A:HEM501 3.1 13.3 0.6 C4A A:HEM501 3.1 14.9 0.4 C1B A:HEM501 3.1 15.5 0.4 C1C A:HEM501 3.1 15.2 0.4 O A:DMS502 3.2 29.3 1.0 CB A:CYS400 3.3 14.1 1.0 CHD A:HEM501 3.4 14.3 0.4 CHA A:HEM501 3.4 14.9 0.4 CHC A:HEM501 3.4 12.9 0.6 CHB A:HEM501 3.4 11.7 0.6 CHA A:HEM501 3.4 12.1 0.6 CHD A:HEM501 3.4 12.8 0.6 CHC A:HEM501 3.5 15.3 0.4 CHB A:HEM501 3.5 15.3 0.4 C2 A:DMS502 3.5 25.0 1.0 C1 A:DMS502 3.6 23.3 1.0 CA A:CYS400 4.0 14.3 1.0 C2D A:HEM501 4.2 14.0 0.4 C3D A:HEM501 4.2 15.1 0.4 C3A A:HEM501 4.2 11.1 0.6 C2A A:HEM501 4.2 12.3 0.6 C3C A:HEM501 4.2 12.8 0.6 C2A A:HEM501 4.3 15.5 0.4 C3A A:HEM501 4.3 15.0 0.4 C2C A:HEM501 4.3 13.6 0.6 C2D A:HEM501 4.3 12.2 0.6 C3D A:HEM501 4.3 12.6 0.6 C3C A:HEM501 4.3 15.8 0.4 C2C A:HEM501 4.3 15.7 0.4 C2B A:HEM501 4.3 15.3 0.4 C3B A:HEM501 4.3 16.2 0.4 C2B A:HEM501 4.3 13.3 0.6 C3B A:HEM501 4.3 14.4 0.6 N A:GLY402 4.8 15.3 1.0 C A:CYS400 4.8 14.9 1.0 CB A:ALA264 5.0 20.7 1.0 N A:ILE401 5.0 14.5 1.0

Iron binding site 2 out of 4 in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine


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 P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:13.0 occ:0.61 FE A:HEM501 0.0 13.0 0.6 FE A:HEM501 0.0 15.4 0.4 ND A:HEM501 1.9 14.3 0.4 ND A:HEM501 1.9 12.7 0.6 NA A:HEM501 2.0 15.5 0.4 NA A:HEM501 2.0 11.4 0.6 NC A:HEM501 2.0 12.1 0.6 NB A:HEM501 2.1 14.8 0.4 NB A:HEM501 2.1 12.6 0.6 NC A:HEM501 2.1 15.0 0.4 SG A:CYS400 2.3 15.0 1.0 S A:DMS502 2.3 22.8 1.0 C1D A:HEM501 2.9 14.7 0.4 C4D A:HEM501 2.9 14.7 0.4 C1D A:HEM501 3.0 12.1 0.6 C4D A:HEM501 3.0 12.2 0.6 C4C A:HEM501 3.0 13.0 0.6 C4B A:HEM501 3.0 15.8 0.4 C1A A:HEM501 3.0 15.1 0.4 C1A A:HEM501 3.0 11.8 0.6 C4B A:HEM501 3.0 13.1 0.6 C1B A:HEM501 3.1 15.5 0.4 C4A A:HEM501 3.1 14.9 0.4 C4A A:HEM501 3.1 12.1 0.6 C1C A:HEM501 3.1 13.3 0.6 C4C A:HEM501 3.1 15.0 0.4 C1B A:HEM501 3.1 12.5 0.6 C1C A:HEM501 3.1 15.2 0.4 O A:DMS502 3.3 29.3 1.0 CB A:CYS400 3.3 14.1 1.0 CHD A:HEM501 3.4 12.8 0.6 CHA A:HEM501 3.4 14.9 0.4 CHD A:HEM501 3.4 14.3 0.4 CHC A:HEM501 3.4 12.9 0.6 CHA A:HEM501 3.4 12.1 0.6 CHC A:HEM501 3.5 15.3 0.4 CHB A:HEM501 3.5 11.7 0.6 CHB A:HEM501 3.5 15.3 0.4 C2 A:DMS502 3.5 25.0 1.0 C1 A:DMS502 3.6 23.3 1.0 CA A:CYS400 4.0 14.3 1.0 C2D A:HEM501 4.2 14.0 0.4 C3C A:HEM501 4.2 12.8 0.6 C3D A:HEM501 4.2 15.1 0.4 C3A A:HEM501 4.2 15.0 0.4 C2A A:HEM501 4.2 12.3 0.6 C2A A:HEM501 4.2 15.5 0.4 C2D A:HEM501 4.2 12.2 0.6 C2C A:HEM501 4.2 13.6 0.6 C3A A:HEM501 4.2 11.1 0.6 C3D A:HEM501 4.3 12.6 0.6 C2B A:HEM501 4.3 15.3 0.4 C3B A:HEM501 4.3 16.2 0.4 C3C A:HEM501 4.3 15.8 0.4 C2C A:HEM501 4.3 15.7 0.4 C3B A:HEM501 4.3 14.4 0.6 C2B A:HEM501 4.3 13.3 0.6 C A:CYS400 4.8 14.9 1.0 N A:GLY402 4.8 15.3 1.0

Iron binding site 3 out of 4 in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:15.7 occ:0.52 FE B:HEM501 0.0 15.7 0.5 FE B:HEM501 0.0 13.0 0.5 ND B:HEM501 1.9 15.2 0.5 NA B:HEM501 2.0 12.5 0.5 ND B:HEM501 2.0 13.1 0.5 NB B:HEM501 2.0 13.2 0.5 NC B:HEM501 2.1 16.4 0.5 NA B:HEM501 2.1 15.7 0.5 NB B:HEM501 2.1 15.2 0.5 NC B:HEM501 2.1 12.5 0.5 SG B:CYS400 2.3 15.3 1.0 S B:DMS502 2.4 24.1 1.0 C1D B:HEM501 2.9 15.8 0.5 C4D B:HEM501 3.0 15.9 0.5 C4B B:HEM501 3.0 13.6 0.5 C1D B:HEM501 3.0 12.3 0.5 C1B B:HEM501 3.0 13.4 0.5 C4C B:HEM501 3.0 17.1 0.5 C4B B:HEM501 3.0 17.0 0.5 C4D B:HEM501 3.0 12.5 0.5 C1A B:HEM501 3.0 13.0 0.5 C4C B:HEM501 3.0 13.8 0.5 C1C B:HEM501 3.0 17.3 0.5 C4A B:HEM501 3.0 12.8 0.5 C1B B:HEM501 3.1 16.7 0.5 C1A B:HEM501 3.1 15.1 0.5 C1C B:HEM501 3.1 13.9 0.5 C4A B:HEM501 3.1 14.6 0.5 O B:DMS502 3.2 30.3 1.0 CB B:CYS400 3.4 14.8 1.0 CHD B:HEM501 3.4 15.5 0.5 CHD B:HEM501 3.4 12.6 0.5 CHC B:HEM501 3.4 17.1 0.5 CHC B:HEM501 3.4 13.7 0.5 CHB B:HEM501 3.4 12.4 0.5 CHA B:HEM501 3.4 15.6 0.5 CHA B:HEM501 3.5 12.9 0.5 CHB B:HEM501 3.5 15.1 0.5 C1 B:DMS502 3.5 23.8 1.0 C2 B:DMS502 3.6 29.9 1.0 CA B:CYS400 4.0 14.8 1.0 C2D B:HEM501 4.2 15.0 0.5 C3D B:HEM501 4.2 16.0 0.5 C3A B:HEM501 4.2 12.4 0.5 C2B B:HEM501 4.2 14.0 0.5 C2A B:HEM501 4.2 13.1 0.5 C3C B:HEM501 4.2 18.5 0.5 C3B B:HEM501 4.2 14.3 0.5 C2C B:HEM501 4.2 18.4 0.5 C3C B:HEM501 4.3 13.2 0.5 C2D B:HEM501 4.3 12.7 0.5 C2C B:HEM501 4.3 13.7 0.5 C3B B:HEM501 4.3 16.8 0.5 C3A B:HEM501 4.3 15.1 0.5 C2B B:HEM501 4.3 15.8 0.5 C3D B:HEM501 4.3 12.9 0.5 C2A B:HEM501 4.3 15.4 0.5 N B:GLY402 4.8 15.4 1.0 C B:CYS400 4.8 15.2 1.0 N B:ILE401 5.0 14.7 1.0 CB B:ALA264 5.0 20.7 1.0

Iron binding site 4 out of 4 in the Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L- Pipecolyl-L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:13.0 occ:0.48 FE B:HEM501 0.0 13.0 0.5 FE B:HEM501 0.0 15.7 0.5 ND B:HEM501 1.9 15.2 0.5 ND B:HEM501 2.0 13.1 0.5 NA B:HEM501 2.0 12.5 0.5 NA B:HEM501 2.0 15.7 0.5 NB B:HEM501 2.0 15.2 0.5 NC B:HEM501 2.0 12.5 0.5 NB B:HEM501 2.1 13.2 0.5 NC B:HEM501 2.1 16.4 0.5 SG B:CYS400 2.2 15.3 1.0 S B:DMS502 2.4 24.1 1.0 C1D B:HEM501 3.0 12.3 0.5 C4D B:HEM501 3.0 15.9 0.5 C1D B:HEM501 3.0 15.8 0.5 C4B B:HEM501 3.0 13.6 0.5 C4B B:HEM501 3.0 17.0 0.5 C4D B:HEM501 3.0 12.5 0.5 C4C B:HEM501 3.0 13.8 0.5 C1B B:HEM501 3.0 16.7 0.5 C1B B:HEM501 3.0 13.4 0.5 C4C B:HEM501 3.0 17.1 0.5 C1A B:HEM501 3.0 13.0 0.5 C1A B:HEM501 3.1 15.1 0.5 C4A B:HEM501 3.1 14.6 0.5 C1C B:HEM501 3.1 17.3 0.5 C1C B:HEM501 3.1 13.9 0.5 C4A B:HEM501 3.1 12.8 0.5 O B:DMS502 3.2 30.3 1.0 CB B:CYS400 3.4 14.8 1.0 CHD B:HEM501 3.4 12.6 0.5 CHC B:HEM501 3.4 17.1 0.5 CHB B:HEM501 3.4 15.1 0.5 CHC B:HEM501 3.4 13.7 0.5 CHD B:HEM501 3.4 15.5 0.5 CHA B:HEM501 3.4 15.6 0.5 CHA B:HEM501 3.5 12.9 0.5 CHB B:HEM501 3.5 12.4 0.5 C1 B:DMS502 3.6 23.8 1.0 C2 B:DMS502 3.6 29.9 1.0 CA B:CYS400 4.0 14.8 1.0 C3C B:HEM501 4.2 13.2 0.5 C2D B:HEM501 4.2 15.0 0.5 C2D B:HEM501 4.2 12.7 0.5 C3D B:HEM501 4.2 16.0 0.5 C2A B:HEM501 4.2 13.1 0.5 C3A B:HEM501 4.3 12.4 0.5 C2B B:HEM501 4.3 14.0 0.5 C2C B:HEM501 4.3 13.7 0.5 C3B B:HEM501 4.3 14.3 0.5 C3C B:HEM501 4.3 18.5 0.5 C2C B:HEM501 4.3 18.4 0.5 C3A B:HEM501 4.3 15.1 0.5 C2B B:HEM501 4.3 15.8 0.5 C3B B:HEM501 4.3 16.8 0.5 C3D B:HEM501 4.3 12.9 0.5 C2A B:HEM501 4.3 15.4 0.5 C B:CYS400 4.8 15.2 1.0 N B:GLY402 4.8 15.4 1.0 N B:ILE401 5.0 14.7 1.0 CB B:ALA264 5.0 20.7 1.0

O.Shoji, K.Yonemura. Crystal Structure of P450BM3 with N-(3-Cyclopentylpropanoyl)-L-Pipecolyl-L-Phenylalanine To Be Published.