Iron in PDB 4zfa: Cytochrome P450 Wild Type From BM3 with Bound Peg

All present enzymatic activity of Cytochrome P450 Wild Type From BM3 with Bound Peg:
1.14.14.1; 1.6.2.4;

The structure of Cytochrome P450 Wild Type From BM3 with Bound Peg, PDB code: 4zfa was solved by W.E.Rogers, T.Othman, D.K.Heidary, T.Huxford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.81 / 2.77
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	55.503, 55.503, 717.749, 90.00, 90.00, 120.00
R / Rfree (%)	24.4 / 30.2

The structure of Cytochrome P450 Wild Type From BM3 with Bound Peg also contains other interesting chemical elements:

Nickel

(Ni)

4 atoms

The binding sites of Iron atom in the Cytochrome P450 Wild Type From BM3 with Bound Peg (pdb code 4zfa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cytochrome P450 Wild Type From BM3 with Bound Peg, PDB code: 4zfa:

Iron binding site 1 out of 1 in the Cytochrome P450 Wild Type From BM3 with Bound Peg


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 Wild Type From BM3 with Bound Peg within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:41.7 occ:1.00 FE A:HEM501 0.0 41.7 1.0 NC A:HEM501 2.1 44.2 1.0 ND A:HEM501 2.1 43.3 1.0 NA A:HEM501 2.1 43.7 1.0 NB A:HEM501 2.1 43.6 1.0 SG A:CYS400 2.5 43.9 1.0 O2 A:EDO503 2.8 44.5 1.0 C4C A:HEM501 3.0 44.3 1.0 C1C A:HEM501 3.0 43.7 1.0 C1D A:HEM501 3.1 43.7 1.0 C4D A:HEM501 3.1 43.8 1.0 C1A A:HEM501 3.1 43.1 1.0 C1B A:HEM501 3.1 43.9 1.0 C4B A:HEM501 3.1 43.5 1.0 C4A A:HEM501 3.1 43.3 1.0 CB A:CYS400 3.2 44.2 1.0 CHD A:HEM501 3.4 44.5 1.0 CHC A:HEM501 3.4 43.3 1.0 CHA A:HEM501 3.4 43.3 1.0 CHB A:HEM501 3.5 43.9 1.0 C2 A:EDO503 3.6 44.7 1.0 CA A:CYS400 4.0 43.4 1.0 C2C A:HEM501 4.2 44.6 1.0 C3C A:HEM501 4.2 44.0 1.0 C2B A:HEM501 4.3 44.0 1.0 C2D A:HEM501 4.3 43.3 1.0 C2A A:HEM501 4.3 43.0 1.0 C3A A:HEM501 4.3 42.7 1.0 C3D A:HEM501 4.3 43.6 1.0 C3B A:HEM501 4.3 43.9 1.0 O A:ALA264 4.6 43.6 1.0 CE2 A:PHE87 4.7 42.9 1.0 C A:CYS400 4.8 44.1 1.0 N A:ILE401 5.0 43.4 1.0

I.Geronimo, C.A.Denning, W.E.Rogers, T.Othman, T.Huxford, D.K.Heidary, E.C.Glazer, C.M.Payne. Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants. Biochemistry V. 55 3594 2016.
ISSN: ISSN 0006-2960
PubMed: 27267136
DOI: 10.1021/ACS.BIOCHEM.6B00183