Iron in PDB 3p3x: Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus

The structure of Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus, PDB code: 3p3x was solved by G.Zocher, M.E.A.Richter, U.Mueller, C.Hertweck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	129.330, 131.780, 53.230, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 28

The structure of Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus (pdb code 3p3x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus, PDB code: 3p3x:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus


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 the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:19.1 occ:1.00 FE A:HEM501 0.0 19.1 1.0 NC A:HEM501 2.1 18.8 1.0 NB A:HEM501 2.1 18.5 1.0 NA A:HEM501 2.1 18.5 1.0 ND A:HEM501 2.1 18.8 1.0 SG A:CYS355 2.3 22.1 1.0 C4C A:HEM501 3.0 19.1 1.0 C1D A:HEM501 3.1 18.6 1.0 C1B A:HEM501 3.1 18.4 1.0 C4A A:HEM501 3.1 18.3 1.0 C1C A:HEM501 3.1 18.9 1.0 C4B A:HEM501 3.1 18.6 1.0 C4D A:HEM501 3.1 18.5 1.0 C1A A:HEM501 3.1 18.6 1.0 CHD A:HEM501 3.4 19.3 1.0 CHB A:HEM501 3.4 18.6 1.0 CB A:CYS355 3.4 20.4 1.0 CHC A:HEM501 3.5 18.5 1.0 CHA A:HEM501 3.5 18.3 1.0 CA A:CYS355 4.1 21.1 1.0 O A:ALA243 4.2 16.8 1.0 C3C A:HEM501 4.3 19.6 1.0 C2C A:HEM501 4.3 19.4 1.0 C2B A:HEM501 4.3 17.9 1.0 C3A A:HEM501 4.3 18.3 1.0 C2D A:HEM501 4.3 18.6 1.0 C3B A:HEM501 4.3 18.1 1.0 C2A A:HEM501 4.3 18.3 1.0 C3D A:HEM501 4.3 18.4 1.0 OG1 A:THR247 4.7 19.8 1.0 CB A:ALA243 4.8 17.1 1.0 C A:CYS355 4.8 21.0 1.0 N A:LEU356 4.8 21.2 1.0 N A:GLY357 4.8 21.0 1.0 C A:ALA243 4.9 17.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus


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 the Cytochrome P450 Monooxygenase Aurh (Nterm- Aurh-I) From Streptomyces Thioluteus within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:21.2 occ:1.00 FE B:HEM501 0.0 21.2 1.0 O B:HOH503 2.0 13.7 1.0 NA B:HEM501 2.0 20.3 1.0 NC B:HEM501 2.1 21.6 1.0 NB B:HEM501 2.1 21.3 1.0 ND B:HEM501 2.1 21.0 1.0 SG B:CYS355 2.4 22.1 1.0 C1A B:HEM501 3.1 20.2 1.0 C4A B:HEM501 3.1 20.0 1.0 C4D B:HEM501 3.1 20.7 1.0 C1C B:HEM501 3.1 21.9 1.0 C4C B:HEM501 3.1 22.0 1.0 C1B B:HEM501 3.1 20.8 1.0 C1D B:HEM501 3.1 20.9 1.0 C4B B:HEM501 3.1 21.7 1.0 CHA B:HEM501 3.4 20.3 1.0 CB B:CYS355 3.4 19.6 1.0 CHB B:HEM501 3.4 20.3 1.0 CHD B:HEM501 3.4 21.6 1.0 CHC B:HEM501 3.5 21.9 1.0 CA B:CYS355 4.1 19.8 1.0 O B:ALA243 4.1 21.7 1.0 C3A B:HEM501 4.3 20.0 1.0 C2A B:HEM501 4.3 19.7 1.0 C2C B:HEM501 4.3 22.7 1.0 C3C B:HEM501 4.3 22.5 1.0 C2B B:HEM501 4.3 21.1 1.0 C3B B:HEM501 4.3 21.6 1.0 C3D B:HEM501 4.3 20.3 1.0 C2D B:HEM501 4.3 20.9 1.0 OG1 B:THR247 4.6 20.1 1.0 N B:LEU356 4.6 20.9 1.0 CB B:ALA243 4.7 20.7 1.0 C B:CYS355 4.7 20.6 1.0 N B:GLY357 4.8 21.7 1.0 C B:ALA243 4.9 21.4 1.0

G.Zocher, M.E.Richter, U.Mueller, C.Hertweck. Structural Fine-Tuning of A Multifunctional Cytochrome P450 Monooxygenase. J.Am.Chem.Soc. V. 133 2292 2011.
ISSN: ISSN 0002-7863
PubMed: 21280577
DOI: 10.1021/JA110146Z