Iron in PDB 4h23: Cytochrome P411BM3-Cis Cyclopropanation Catalyst

All present enzymatic activity of Cytochrome P411BM3-Cis Cyclopropanation Catalyst:
1.14.14.1;

The structure of Cytochrome P411BM3-Cis Cyclopropanation Catalyst, PDB code: 4h23 was solved by P.S.Coelho, Z.J.Wang, M.E.Ener, S.A.Baril, A.Kannan, F.H.Arnold, E.M.Brustad, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.90 / 3.30
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.158, 124.455, 127.691, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 26.5

The binding sites of Iron atom in the Cytochrome P411BM3-Cis Cyclopropanation Catalyst (pdb code 4h23). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome P411BM3-Cis Cyclopropanation Catalyst, PDB code: 4h23:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cytochrome P411BM3-Cis Cyclopropanation Catalyst


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P411BM3-Cis Cyclopropanation Catalyst within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:22.9 occ:1.00 FE A:HEM500 0.0 22.9 1.0 NB A:HEM500 2.0 21.5 1.0 NA A:HEM500 2.0 23.7 1.0 ND A:HEM500 2.0 22.7 1.0 NC A:HEM500 2.1 21.4 1.0 OG A:SER400 2.1 23.0 1.0 CB A:SER400 2.9 25.2 1.0 C4B A:HEM500 3.0 21.6 1.0 C1D A:HEM500 3.0 22.3 1.0 C4D A:HEM500 3.0 23.4 1.0 C1A A:HEM500 3.0 24.1 1.0 C1C A:HEM500 3.1 20.5 1.0 C4A A:HEM500 3.1 23.0 1.0 C1B A:HEM500 3.1 22.0 1.0 C4C A:HEM500 3.1 19.9 1.0 CHC A:HEM500 3.4 21.3 1.0 CHA A:HEM500 3.4 23.3 1.0 CHD A:HEM500 3.4 20.3 1.0 CHB A:HEM500 3.4 21.7 1.0 CA A:SER400 3.7 25.9 1.0 C2D A:HEM500 4.3 23.3 1.0 C3B A:HEM500 4.3 21.9 1.0 C3A A:HEM500 4.3 23.3 1.0 C2C A:HEM500 4.3 19.1 1.0 C3C A:HEM500 4.3 20.5 1.0 C3D A:HEM500 4.3 23.7 1.0 C2A A:HEM500 4.3 24.6 1.0 C2B A:HEM500 4.3 21.5 1.0 C A:SER400 4.7 27.2 1.0 N A:GLY402 4.7 31.0 1.0 N A:SER400 4.8 25.9 1.0 CA A:GLY402 4.9 31.4 1.0 N A:ILE401 4.9 28.5 1.0

Iron binding site 2 out of 2 in the Cytochrome P411BM3-Cis Cyclopropanation Catalyst


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome P411BM3-Cis Cyclopropanation Catalyst within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:31.9 occ:1.00 FE B:HEM500 0.0 31.9 1.0 ND B:HEM500 2.0 30.8 1.0 NA B:HEM500 2.0 31.3 1.0 NB B:HEM500 2.0 31.5 1.0 OG B:SER400 2.1 25.4 1.0 NC B:HEM500 2.2 31.9 1.0 CB B:SER400 2.9 28.0 1.0 C1D B:HEM500 3.0 30.4 1.0 C4D B:HEM500 3.0 32.4 1.0 C1B B:HEM500 3.0 30.6 1.0 C4A B:HEM500 3.0 30.1 1.0 C1A B:HEM500 3.1 31.9 1.0 C4B B:HEM500 3.1 31.0 1.0 C4C B:HEM500 3.1 30.8 1.0 C1C B:HEM500 3.2 31.7 1.0 CHB B:HEM500 3.4 30.3 1.0 CHA B:HEM500 3.4 33.0 1.0 CHD B:HEM500 3.4 29.5 1.0 CHC B:HEM500 3.5 30.9 1.0 CA B:SER400 3.6 29.1 1.0 C2D B:HEM500 4.2 32.8 1.0 C2B B:HEM500 4.2 29.5 1.0 C3D B:HEM500 4.2 34.0 1.0 C3B B:HEM500 4.3 30.7 1.0 C3A B:HEM500 4.3 28.8 1.0 C2A B:HEM500 4.3 29.9 1.0 C3C B:HEM500 4.4 31.3 1.0 C2C B:HEM500 4.4 31.1 1.0 C B:SER400 4.6 30.1 1.0 O B:ALA264 4.7 32.6 1.0 N B:SER400 4.7 30.2 1.0 N B:ILE401 4.8 30.2 1.0

P.S.Coelho, Z.J.Wang, M.E.Ener, S.A.Baril, A.Kannan, F.H.Arnold, E.M.Brustad. A Serine-Substituted P450 Catalyzes Highly Efficient Carbene Transfer to Olefins in Vivo. Nat.Chem.Biol. V. 9 485 2013.
ISSN: ISSN 1552-4450
PubMed: 23792734
DOI: 10.1038/NCHEMBIO.1278