Iron in PDB 3mgx: Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics

All present enzymatic activity of Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics:
1.14.14.1;

The structure of Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics, PDB code: 3mgx was solved by M.J.Cryle, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.75 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.850, 61.050, 100.640, 90.00, 102.48, 90.00
R / Rfree (%)	20.8 / 23.3

The binding sites of Iron atom in the Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics (pdb code 3mgx). 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 P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics, PDB code: 3mgx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics


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 P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe397 b:28.0 occ:1.00 FE A:HEM397 0.0 28.0 1.0 O A:HOH448 2.0 25.0 1.0 NA A:HEM397 2.1 28.9 1.0 NC A:HEM397 2.1 28.1 1.0 NB A:HEM397 2.1 28.2 1.0 ND A:HEM397 2.1 28.6 1.0 SG A:CYS345 2.4 29.9 1.0 C4C A:HEM397 3.1 28.4 1.0 C1A A:HEM397 3.1 29.3 1.0 C4A A:HEM397 3.1 29.0 1.0 C1C A:HEM397 3.1 28.2 1.0 C1B A:HEM397 3.1 28.0 1.0 C4B A:HEM397 3.1 27.8 1.0 C1D A:HEM397 3.1 28.8 1.0 C4D A:HEM397 3.1 29.0 1.0 CB A:CYS345 3.4 30.5 1.0 CHB A:HEM397 3.4 28.4 1.0 CHD A:HEM397 3.4 28.7 1.0 CHC A:HEM397 3.4 28.1 1.0 CHA A:HEM397 3.4 29.1 1.0 CA A:CYS345 4.1 31.2 1.0 O A:GLY235 4.1 30.0 1.0 O3 A:GOL399 4.1 53.3 1.0 C3C A:HEM397 4.3 28.4 1.0 C2C A:HEM397 4.3 28.3 1.0 C2A A:HEM397 4.3 29.8 1.0 C3A A:HEM397 4.3 29.5 1.0 C2B A:HEM397 4.3 27.9 1.0 C3B A:HEM397 4.3 27.7 1.0 C3D A:HEM397 4.4 28.9 1.0 C2D A:HEM397 4.4 29.1 1.0 C A:GLY235 4.7 30.3 1.0 C A:CYS345 4.7 31.4 1.0 N A:GLY347 4.8 30.6 1.0 N A:LEU346 4.8 31.5 1.0 CA A:GLY235 4.8 30.6 1.0 O1 A:GOL399 4.8 53.8 1.0 OG1 A:THR239 4.9 30.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics


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 P450 Oxyd That Is Involved in the Biosynthesis of Vancomycin-Type Antibiotics within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe397 b:18.1 occ:1.00 FE B:HEM397 0.0 18.1 1.0 O B:HOH498 2.0 21.4 1.0 NB B:HEM397 2.0 17.4 1.0 NA B:HEM397 2.1 18.0 1.0 ND B:HEM397 2.1 17.9 1.0 NC B:HEM397 2.1 17.8 1.0 SG B:CYS345 2.3 18.3 1.0 C1A B:HEM397 3.1 18.4 1.0 C4B B:HEM397 3.1 17.5 1.0 C4D B:HEM397 3.1 18.8 1.0 C1B B:HEM397 3.1 17.4 1.0 C4A B:HEM397 3.1 17.9 1.0 C1C B:HEM397 3.1 17.6 1.0 C4C B:HEM397 3.1 17.7 1.0 C1D B:HEM397 3.1 18.3 1.0 CB B:CYS345 3.4 19.6 1.0 CHA B:HEM397 3.4 18.0 1.0 CHC B:HEM397 3.4 17.3 1.0 CHB B:HEM397 3.4 17.4 1.0 CHD B:HEM397 3.5 17.2 1.0 O B:GLY235 4.0 18.4 1.0 CA B:CYS345 4.1 20.4 1.0 O2 B:GOL399 4.2 48.6 1.0 C2A B:HEM397 4.3 18.5 1.0 C3B B:HEM397 4.3 16.9 1.0 C2B B:HEM397 4.3 17.2 1.0 C3A B:HEM397 4.3 17.9 1.0 C2C B:HEM397 4.3 18.0 1.0 C3D B:HEM397 4.3 18.8 1.0 C3C B:HEM397 4.3 18.2 1.0 C2D B:HEM397 4.3 18.3 1.0 C1 B:GOL399 4.5 49.0 1.0 C B:GLY235 4.7 18.6 1.0 N B:GLY347 4.7 21.3 1.0 C B:CYS345 4.8 20.9 1.0 CA B:GLY235 4.8 18.9 1.0 C2 B:GOL399 4.8 49.0 1.0 N B:LEU346 4.9 21.3 1.0 OG1 B:THR239 4.9 19.2 1.0

M.J.Cryle, A.Meinhart, I.Schlichting. Structural Characterization of Oxyd, A Cytochrome P450 Involved in {Beta}-Hydroxytyrosine Formation in Vancomycin Biosynthesis J.Biol.Chem. V. 285 24562 2010.
ISSN: ISSN 0021-9258
PubMed: 20519494
DOI: 10.1074/JBC.M110.131904