Iron in PDB 6hqw: Cytochrome P450-153 From Novosphingobium Aromaticivorans

The structure of Cytochrome P450-153 From Novosphingobium Aromaticivorans, PDB code: 6hqw 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)	97.98 / 2.90
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	113.133, 113.133, 72.970, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 29.9

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

Iron binding site 1 out of 2 in the Cytochrome P450-153 From Novosphingobium Aromaticivorans


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 Novosphingobium Aromaticivorans within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:45.0 occ:1.00 FE A:HEM500 0.0 45.0 1.0 ND A:HEM500 1.9 44.7 1.0 NA A:HEM500 2.0 41.8 1.0 NB A:HEM500 2.1 43.9 1.0 NC A:HEM500 2.1 43.6 1.0 SG A:CYS394 2.4 35.9 1.0 C1D A:HEM500 2.9 42.8 1.0 C4D A:HEM500 2.9 40.5 1.0 C1A A:HEM500 2.9 38.3 1.0 C4A A:HEM500 3.0 44.7 1.0 C1B A:HEM500 3.0 44.2 1.0 C4B A:HEM500 3.0 45.9 1.0 C4C A:HEM500 3.0 43.9 1.0 C1C A:HEM500 3.1 45.9 1.0 CHA A:HEM500 3.3 39.1 1.0 CHD A:HEM500 3.3 44.1 1.0 CHB A:HEM500 3.4 44.8 1.0 CHC A:HEM500 3.5 45.7 1.0 CB A:CYS394 3.6 36.9 1.0 C2A A:HEM500 4.1 40.2 1.0 C2D A:HEM500 4.1 41.6 1.0 C3D A:HEM500 4.1 38.9 1.0 CA A:CYS394 4.1 37.6 1.0 C3A A:HEM500 4.2 41.9 1.0 C2B A:HEM500 4.2 45.0 1.0 C3C A:HEM500 4.3 46.9 1.0 C3B A:HEM500 4.3 47.0 1.0 O A:GLY283 4.3 87.8 1.0 C2C A:HEM500 4.3 48.9 1.0 CA A:GLY283 4.8 74.7 1.0 C A:GLY283 4.8 76.1 1.0 N A:VAL395 4.9 43.9 1.0 N A:GLY396 4.9 53.9 1.0 C A:CYS394 4.9 40.5 1.0

Iron binding site 2 out of 2 in the Cytochrome P450-153 From Novosphingobium Aromaticivorans


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 Novosphingobium Aromaticivorans within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:100.0 occ:1.00 FE B:HEM500 0.0 100.0 1.0 ND B:HEM500 1.9 98.3 1.0 NA B:HEM500 2.0 89.8 1.0 SG B:CYS394 2.1 80.6 1.0 NC B:HEM500 2.1 89.0 1.0 NB B:HEM500 2.1 97.6 1.0 C4D B:HEM500 2.9 96.7 1.0 C1D B:HEM500 2.9 91.9 1.0 C1A B:HEM500 3.0 92.6 1.0 C4A B:HEM500 3.0 91.3 1.0 C4C B:HEM500 3.0 95.1 1.0 C1B B:HEM500 3.1 93.9 1.0 C4B B:HEM500 3.1 0.6 1.0 C1C B:HEM500 3.1 90.0 1.0 CB B:CYS394 3.3 81.2 1.0 CHA B:HEM500 3.3 97.8 1.0 CHD B:HEM500 3.4 98.4 1.0 CHB B:HEM500 3.4 92.4 1.0 CHC B:HEM500 3.5 94.0 1.0 O B:GLY283 3.7 93.4 1.0 CA B:CYS394 3.9 85.5 1.0 C3D B:HEM500 4.1 90.1 1.0 C2D B:HEM500 4.1 92.5 1.0 C3A B:HEM500 4.2 91.7 1.0 C2A B:HEM500 4.2 86.9 1.0 C3C B:HEM500 4.3 94.8 1.0 C2C B:HEM500 4.3 95.6 1.0 C2B B:HEM500 4.3 95.1 1.0 C3B B:HEM500 4.3 99.9 1.0 C B:GLY283 4.4 93.4 1.0 CA B:GLY283 4.5 92.8 1.0 C B:CYS394 4.8 89.2 1.0 OG1 B:THR287 4.9 93.9 1.0 N B:VAL395 4.9 97.0 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