Iron in PDB 5e9z: Cytochrome P450 BM3 Mutant M11

All present enzymatic activity of Cytochrome P450 BM3 Mutant M11:
1.14.14.1; 1.6.2.4;

The structure of Cytochrome P450 BM3 Mutant M11, PDB code: 5e9z was solved by L.Capoferri, R.Leth, E.Ter Haar, A.K.Mohanty, D.J.Grootenhuis, E.Vottero, J.N.M.Commandeur, N.P.E.Vermeulen, F.S.Jorgensen, L.Olsen, D.P.Geerke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	95.12 / 2.23
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	379.122, 59.720, 95.587, 90.00, 95.67, 90.00
R / Rfree (%)	18.8 / 22.5

The binding sites of Iron atom in the Cytochrome P450 BM3 Mutant M11 (pdb code 5e9z). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome P450 BM3 Mutant M11, PDB code: 5e9z:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome P450 BM3 Mutant M11


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 BM3 Mutant M11 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:16.8 occ:1.00 NB A:PP9502 2.0 16.1 1.0 NC A:PP9502 2.0 13.7 1.0 ND A:PP9502 2.1 11.0 1.0 NA A:PP9502 2.1 15.9 1.0 SG A:CYS400 2.3 20.1 1.0 O A:HOH778 2.6 22.5 1.0 C4B A:PP9502 3.0 17.0 1.0 C4C A:PP9502 3.0 11.5 1.0 C1B A:PP9502 3.0 17.0 1.0 C1D A:PP9502 3.0 14.4 1.0 C1C A:PP9502 3.1 17.9 1.0 C4A A:PP9502 3.1 17.1 1.0 C4D A:PP9502 3.1 13.7 1.0 C1A A:PP9502 3.2 15.7 1.0 CHD A:PP9502 3.4 12.6 1.0 CHB A:PP9502 3.4 16.8 1.0 CHC A:PP9502 3.4 18.1 1.0 CB A:CYS400 3.4 18.0 1.0 CHA A:PP9502 3.5 13.5 1.0 CA A:CYS400 4.2 19.1 1.0 C3C A:PP9502 4.3 18.5 1.0 C3B A:PP9502 4.3 15.5 1.0 C2C A:PP9502 4.3 16.6 1.0 C2B A:PP9502 4.3 15.9 1.0 C2D A:PP9502 4.3 17.2 1.0 C3A A:PP9502 4.3 15.3 1.0 C3D A:PP9502 4.4 16.7 1.0 C2A A:PP9502 4.4 17.4 1.0 HHD A:PP9502 4.4 12.4 1.0 HHC A:PP9502 4.5 17.0 1.0 HHB A:PP9502 4.5 16.4 1.0 HHA A:PP9502 4.6 12.7 1.0 O A:ALA264 4.8 25.8 1.0 OG1 A:THR268 4.9 21.0 1.0 N A:GLY402 5.0 17.4 1.0 C A:CYS400 5.0 24.1 1.0

Iron binding site 2 out of 4 in the Cytochrome P450 BM3 Mutant M11


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome P450 BM3 Mutant M11 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe503 b:21.5 occ:1.00 NC B:PP9502 2.0 16.8 1.0 NA B:PP9502 2.0 13.9 1.0 ND B:PP9502 2.1 13.8 1.0 NB B:PP9502 2.1 16.4 1.0 SG B:CYS400 2.3 18.4 1.0 O B:HOH793 2.9 27.1 1.0 C4D B:PP9502 3.0 14.3 1.0 C1C B:PP9502 3.1 20.1 1.0 C1A B:PP9502 3.1 15.1 1.0 C4C B:PP9502 3.1 13.1 1.0 C1D B:PP9502 3.1 12.4 1.0 C4A B:PP9502 3.1 15.4 1.0 C4B B:PP9502 3.1 16.7 1.0 C1B B:PP9502 3.2 14.8 1.0 CB B:CYS400 3.3 14.7 1.0 CHC B:PP9502 3.4 18.4 1.0 CHA B:PP9502 3.4 17.3 1.0 CHD B:PP9502 3.4 14.8 1.0 CHB B:PP9502 3.5 16.8 1.0 CA B:CYS400 4.0 15.5 1.0 C3C B:PP9502 4.3 13.0 1.0 C2C B:PP9502 4.3 16.2 1.0 C3D B:PP9502 4.3 12.9 1.0 C2A B:PP9502 4.3 16.0 1.0 C2D B:PP9502 4.3 14.9 1.0 C3A B:PP9502 4.3 15.4 1.0 C3B B:PP9502 4.3 16.4 1.0 C2B B:PP9502 4.4 15.8 1.0 HHC B:PP9502 4.5 18.6 1.0 HHA B:PP9502 4.5 17.5 1.0 HHD B:PP9502 4.5 14.9 1.0 O B:HOH866 4.5 45.7 1.0 HHB B:PP9502 4.6 16.8 1.0 C B:CYS400 4.8 19.5 1.0 N B:GLY402 4.9 16.1 1.0 N B:ILE401 4.9 16.2 1.0 O B:ALA264 4.9 21.1 1.0

Iron binding site 3 out of 4 in the Cytochrome P450 BM3 Mutant M11


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome P450 BM3 Mutant M11 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:22.4 occ:1.00 NB C:PP9501 2.0 19.0 1.0 NC C:PP9501 2.1 21.6 1.0 ND C:PP9501 2.1 19.9 1.0 NA C:PP9501 2.1 24.0 1.0 SG C:CYS400 2.3 24.5 1.0 O C:HOH691 2.4 26.5 1.0 C4B C:PP9501 3.0 19.9 1.0 C1C C:PP9501 3.0 21.8 1.0 C4D C:PP9501 3.1 18.6 1.0 C1B C:PP9501 3.1 18.2 1.0 C4C C:PP9501 3.1 23.5 1.0 C4A C:PP9501 3.1 21.0 1.0 C1A C:PP9501 3.1 21.7 1.0 C1D C:PP9501 3.1 21.7 1.0 CHC C:PP9501 3.3 20.3 1.0 CB C:CYS400 3.4 21.2 1.0 CHA C:PP9501 3.4 14.3 1.0 CHB C:PP9501 3.5 18.2 1.0 CHD C:PP9501 3.5 22.4 1.0 CA C:CYS400 4.1 21.2 1.0 C3B C:PP9501 4.3 21.5 1.0 C2C C:PP9501 4.3 23.4 1.0 C2B C:PP9501 4.3 22.9 1.0 C3C C:PP9501 4.3 25.0 1.0 C3D C:PP9501 4.3 20.8 1.0 C2D C:PP9501 4.4 22.9 1.0 C2A C:PP9501 4.4 22.2 1.0 C3A C:PP9501 4.4 23.1 1.0 HHC C:PP9501 4.4 20.8 1.0 HHA C:PP9501 4.5 13.8 1.0 HHB C:PP9501 4.5 18.3 1.0 HHD C:PP9501 4.6 21.9 1.0 O C:HOH826 4.7 60.6 1.0 OG1 C:THR268 4.8 34.6 1.0 O C:ALA264 4.8 24.3 1.0 C C:CYS400 4.9 24.4 1.0 N C:ILE401 4.9 22.5 1.0 N C:GLY402 5.0 26.4 1.0

Iron binding site 4 out of 4 in the Cytochrome P450 BM3 Mutant M11


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome P450 BM3 Mutant M11 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe502 b:20.4 occ:1.00 ND D:PP9501 2.0 20.6 1.0 NC D:PP9501 2.1 20.6 1.0 NA D:PP9501 2.1 23.4 1.0 NB D:PP9501 2.1 22.4 1.0 SG D:CYS400 2.3 19.4 1.0 O D:HOH763 2.7 24.3 1.0 C4D D:PP9501 3.0 21.1 1.0 C1C D:PP9501 3.1 18.0 1.0 C4B D:PP9501 3.1 21.3 1.0 C1A D:PP9501 3.1 22.8 1.0 C1D D:PP9501 3.1 22.3 1.0 C4C D:PP9501 3.1 23.0 1.0 C4A D:PP9501 3.1 20.2 1.0 C1B D:PP9501 3.1 21.1 1.0 CB D:CYS400 3.4 15.3 1.0 CHC D:PP9501 3.4 21.4 1.0 CHA D:PP9501 3.4 22.1 1.0 CHD D:PP9501 3.5 22.1 1.0 CHB D:PP9501 3.5 19.4 1.0 CA D:CYS400 4.0 15.6 1.0 C3D D:PP9501 4.3 19.6 1.0 C2C D:PP9501 4.3 14.7 1.0 C3C D:PP9501 4.3 21.5 1.0 C3B D:PP9501 4.3 22.6 1.0 C2D D:PP9501 4.3 20.9 1.0 C2A D:PP9501 4.3 22.8 1.0 C2B D:PP9501 4.4 23.8 1.0 C3A D:PP9501 4.4 20.1 1.0 O D:HOH820 4.4 40.1 1.0 HHC D:PP9501 4.5 21.0 1.0 HHA D:PP9501 4.5 21.7 1.0 HHD D:PP9501 4.5 22.1 1.0 HHB D:PP9501 4.6 19.2 1.0 C D:CYS400 4.9 21.1 1.0 N D:GLY402 4.9 20.9 1.0 N D:ILE401 4.9 18.7 1.0 O D:ALA264 4.9 20.0 1.0 OG1 D:THR268 4.9 32.0 1.0

L.Capoferri, R.Leth, E.Ter Haar, A.K.Mohanty, P.D.Grootenhuis, E.Vottero, J.N.Commandeur, N.P.Vermeulen, F.S.Jrgensen, L.Olsen, D.P.Geerke. Insights Into Regioselective Metabolism of Mefenamic Acid By Cytochrome P450 BM3 Mutants Through Crystallography, Docking, Molecular Dynamics, and Free Energy Calculations. Proteins V. 84 383 2016.
ISSN: ESSN 1097-0134
PubMed: 26757175
DOI: 10.1002/PROT.24985