Iron in PDB 3rwl: Structure of P450PYR Hydroxylase

All present enzymatic activity of Structure of P450PYR Hydroxylase:
1.14.15.3;

The structure of Structure of P450PYR Hydroxylase, PDB code: 3rwl was solved by G.Pompidor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.76 / 2.00
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	112.604, 112.604, 41.964, 90.00, 90.00, 120.00
R / Rfree (%)	16 / 19.6

The binding sites of Iron atom in the Structure of P450PYR Hydroxylase (pdb code 3rwl). 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 Structure of P450PYR Hydroxylase, PDB code: 3rwl:

Iron binding site 1 out of 1 in the Structure of P450PYR Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of P450PYR Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe417 b:23.3 occ:1.00 FE A:HEM417 0.0 23.3 1.0 NB A:HEM417 2.0 15.5 1.0 NC A:HEM417 2.1 15.4 1.0 ND A:HEM417 2.1 15.7 1.0 NA A:HEM417 2.2 12.7 1.0 SG A:CYS366 2.3 14.6 1.0 O A:HOH644 2.5 30.2 1.0 C4B A:HEM417 3.0 15.4 1.0 C4C A:HEM417 3.0 22.5 1.0 C1C A:HEM417 3.0 16.2 1.0 C1B A:HEM417 3.1 16.8 1.0 C1D A:HEM417 3.1 20.4 1.0 C4D A:HEM417 3.1 18.6 1.0 C1A A:HEM417 3.1 16.8 1.0 C4A A:HEM417 3.1 15.9 1.0 CHC A:HEM417 3.4 14.8 1.0 CHD A:HEM417 3.4 19.1 1.0 CHA A:HEM417 3.4 11.6 1.0 CB A:CYS366 3.4 17.6 1.0 CHB A:HEM417 3.4 15.1 1.0 CA A:CYS366 4.0 17.3 1.0 O A:GLY255 4.1 18.5 1.0 C3B A:HEM417 4.2 14.2 1.0 C2B A:HEM417 4.2 16.2 1.0 C3C A:HEM417 4.2 18.2 1.0 C2C A:HEM417 4.3 17.7 1.0 C3D A:HEM417 4.3 14.3 1.0 C2D A:HEM417 4.3 17.7 1.0 C2A A:HEM417 4.4 10.1 1.0 C3A A:HEM417 4.4 11.0 1.0 N A:GLY368 4.6 17.4 1.0 C A:GLY255 4.6 17.7 1.0 N A:VAL367 4.8 17.5 1.0 C A:CYS366 4.8 19.3 1.0 CA A:GLY255 4.9 18.7 1.0 CA A:GLY368 5.0 18.2 1.0

S.Q.Pham, G.Pompidor, J.Liu, X.D.Li, Z.Li. Evolving P450PYR Hydroxylase For Highly Enantioselective Hydroxylation at Non-Activated Carbon Atom. Chem.Commun.(Camb.) V. 48 4618 2012.
ISSN: ISSN 1359-7345
PubMed: 22430002
DOI: 10.1039/C2CC30779K