Iron in PDB 6hqd: Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim

The structure of Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim, PDB code: 6hqd was solved by F.Fiorentini, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.311, 96.642, 87.777, 90.00, 119.18, 90.00
R / Rfree (%)	17 / 20

The binding sites of Iron atom in the Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim (pdb code 6hqd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim, PDB code: 6hqd:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:18.2 occ:1.00 FE A:HEM501 0.0 18.2 1.0 O A:HOH613 1.9 25.3 1.0 ND A:HEM501 2.0 17.4 1.0 NA A:HEM501 2.0 16.7 1.0 NC A:HEM501 2.1 19.1 1.0 NB A:HEM501 2.1 17.9 1.0 SG A:CYS370 2.3 20.7 1.0 C4D A:HEM501 3.0 17.8 1.0 C1D A:HEM501 3.0 17.9 1.0 C1A A:HEM501 3.0 16.8 1.0 C4C A:HEM501 3.0 19.7 1.0 C4B A:HEM501 3.0 18.8 1.0 C4A A:HEM501 3.1 16.5 1.0 C1B A:HEM501 3.1 16.7 1.0 C1C A:HEM501 3.1 20.0 1.0 CHA A:HEM501 3.4 17.8 1.0 CHD A:HEM501 3.4 18.2 1.0 CB A:CYS370 3.4 21.3 1.0 CHC A:HEM501 3.5 18.8 1.0 CHB A:HEM501 3.5 16.1 1.0 CA A:CYS370 4.0 20.9 1.0 O A:GLY259 4.2 28.2 1.0 C3C A:HEM501 4.3 21.7 1.0 C2C A:HEM501 4.3 20.6 1.0 C2A A:HEM501 4.3 15.8 1.0 C3A A:HEM501 4.3 17.2 1.0 C2B A:HEM501 4.3 18.4 1.0 C3B A:HEM501 4.3 17.5 1.0 C2D A:HEM501 4.3 18.0 1.0 C3D A:HEM501 4.3 16.6 1.0 N A:LEU371 4.6 18.8 1.0 C A:CYS370 4.7 19.8 1.0 C6 A:PGE503 4.7 37.1 1.0 N A:GLY372 4.7 18.9 1.0 C A:GLY259 5.0 26.6 1.0

Iron binding site 2 out of 3 in the Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:17.2 occ:1.00 FE B:HEM501 0.0 17.2 1.0 ND B:HEM501 1.9 18.0 1.0 NA B:HEM501 2.0 16.3 1.0 NC B:HEM501 2.1 16.9 1.0 NB B:HEM501 2.1 17.9 1.0 O B:HOH686 2.2 28.5 1.0 SG B:CYS370 2.4 20.1 1.0 C1D B:HEM501 3.0 18.2 1.0 C4D B:HEM501 3.0 17.2 1.0 C4B B:HEM501 3.0 17.9 1.0 C4C B:HEM501 3.0 19.6 1.0 C1A B:HEM501 3.0 16.5 1.0 C4A B:HEM501 3.1 16.9 1.0 C1B B:HEM501 3.1 18.0 1.0 C1C B:HEM501 3.1 18.6 1.0 CHD B:HEM501 3.4 18.0 1.0 CHA B:HEM501 3.4 16.7 1.0 CB B:CYS370 3.4 16.5 1.0 CHC B:HEM501 3.4 18.6 1.0 CHB B:HEM501 3.5 16.5 1.0 CA B:CYS370 4.0 16.6 1.0 C3C B:HEM501 4.2 20.1 1.0 C2D B:HEM501 4.3 17.0 1.0 C3D B:HEM501 4.3 16.3 1.0 C3A B:HEM501 4.3 17.2 1.0 C2A B:HEM501 4.3 16.0 1.0 C3B B:HEM501 4.3 17.8 1.0 C2B B:HEM501 4.3 17.6 1.0 C2C B:HEM501 4.3 18.4 1.0 C6 B:PGE503 4.4 40.0 1.0 O B:GLY259 4.4 25.8 1.0 N B:LEU371 4.6 17.7 1.0 N B:GLY372 4.7 17.4 1.0 C B:CYS370 4.7 16.8 1.0 O4 B:PGE503 5.0 41.9 1.0

Iron binding site 3 out of 3 in the Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome P450-153 From Pseudomonas Sp. 19-Rlim within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:17.6 occ:1.00 FE C:HEM501 0.0 17.6 1.0 ND C:HEM501 2.0 16.5 1.0 NA C:HEM501 2.0 15.5 1.0 NC C:HEM501 2.1 16.7 1.0 NB C:HEM501 2.1 17.8 1.0 SG C:CYS370 2.3 19.9 1.0 O C:HOH700 2.4 32.1 1.0 C1D C:HEM501 3.0 16.3 1.0 C4B C:HEM501 3.0 17.4 1.0 C4D C:HEM501 3.0 15.2 1.0 C1A C:HEM501 3.1 16.1 1.0 C4C C:HEM501 3.1 17.9 1.0 C1C C:HEM501 3.1 17.9 1.0 C4A C:HEM501 3.1 16.8 1.0 C1B C:HEM501 3.1 17.8 1.0 CB C:CYS370 3.4 18.8 1.0 CHC C:HEM501 3.4 19.5 1.0 CHD C:HEM501 3.4 17.1 1.0 CHA C:HEM501 3.5 15.3 1.0 CHB C:HEM501 3.5 18.0 1.0 CA C:CYS370 4.0 17.4 1.0 C2D C:HEM501 4.3 15.8 1.0 C3A C:HEM501 4.3 15.2 1.0 C3B C:HEM501 4.3 18.9 1.0 C3D C:HEM501 4.3 14.9 1.0 C2B C:HEM501 4.3 17.3 1.0 C3C C:HEM501 4.3 19.1 1.0 C2A C:HEM501 4.3 15.7 1.0 C2C C:HEM501 4.3 17.9 1.0 N C:GLY372 4.7 19.1 1.0 N C:LEU371 4.7 18.6 1.0 C C:CYS370 4.7 18.0 1.0 O C:GLY259 4.7 28.2 1.0 OG1 C:THR263 5.0 26.9 1.0 O1 C:PGE504 5.0 44.5 1.0

F.Fiorentini, A.M.Hatzl, S.Schmidt, S.Savino, A.Glieder, A.Mattevi. The Extreme Structural Plasticity in the CYP153 Subfamily of P450S Directs Development of Designer Hydroxylases. Biochemistry V. 57 6701 2018.
ISSN: ISSN 0006-2960
PubMed: 30398864
DOI: 10.1021/ACS.BIOCHEM.8B01052