Iron in PDB 1io9: Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties

The structure of Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties, PDB code: 1io9 was solved by S.-Y.Park, K.Yamane, S.Adachi, Y.Shiro, S.G.Sligar, Rikenstructural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.05
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	87.587, 87.587, 223.151, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 28.4

The binding sites of Iron atom in the Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties (pdb code 1io9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties, PDB code: 1io9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:22.5 occ:1.00 FE A:HEM401 0.0 22.5 1.0 O A:HOH402 1.8 22.0 1.0 NC A:HEM401 2.0 18.9 1.0 ND A:HEM401 2.0 27.6 1.0 NA A:HEM401 2.0 17.6 1.0 NB A:HEM401 2.0 24.2 1.0 SG A:CYS317 2.1 26.2 1.0 C1C A:HEM401 3.0 25.0 1.0 C4D A:HEM401 3.0 24.2 1.0 C4C A:HEM401 3.0 27.2 1.0 C4B A:HEM401 3.0 21.4 1.0 C1D A:HEM401 3.0 21.0 1.0 C1A A:HEM401 3.1 25.2 1.0 C1B A:HEM401 3.1 17.9 1.0 C4A A:HEM401 3.1 20.6 1.0 CB A:CYS317 3.3 19.8 1.0 CHA A:HEM401 3.4 24.5 1.0 CHC A:HEM401 3.4 24.5 1.0 CHD A:HEM401 3.4 21.4 1.0 CHB A:HEM401 3.5 19.6 1.0 CA A:CYS317 4.0 22.9 1.0 C3B A:HEM401 4.3 24.8 1.0 C3D A:HEM401 4.3 23.4 1.0 C2C A:HEM401 4.3 22.6 1.0 C3C A:HEM401 4.3 23.6 1.0 C2B A:HEM401 4.3 22.4 1.0 C2D A:HEM401 4.3 26.4 1.0 C2A A:HEM401 4.3 25.1 1.0 C3A A:HEM401 4.4 21.4 1.0 O A:ALA209 4.5 24.0 1.0 C A:CYS317 4.6 26.5 1.0 N A:LEU318 4.7 27.8 1.0 N A:GLY319 4.8 24.6 1.0

Iron binding site 2 out of 2 in the Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structural Origin of Its Thermostability and Functional Properties within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:20.9 occ:1.00 FE B:HEM901 0.0 20.9 1.0 O B:HOH902 1.8 14.6 1.0 NC B:HEM901 2.0 22.8 1.0 NB B:HEM901 2.0 23.1 1.0 NA B:HEM901 2.0 21.8 1.0 ND B:HEM901 2.0 25.9 1.0 SG B:CYS817 2.1 20.9 1.0 C1C B:HEM901 3.0 23.0 1.0 C4B B:HEM901 3.0 22.1 1.0 C4C B:HEM901 3.0 26.4 1.0 C1A B:HEM901 3.1 23.4 1.0 C4D B:HEM901 3.1 25.3 1.0 C4A B:HEM901 3.1 20.1 1.0 C1B B:HEM901 3.1 24.7 1.0 C1D B:HEM901 3.1 24.4 1.0 CB B:CYS817 3.3 20.4 1.0 CHC B:HEM901 3.4 25.5 1.0 CHA B:HEM901 3.5 25.0 1.0 CHD B:HEM901 3.5 24.0 1.0 CHB B:HEM901 3.5 25.8 1.0 CA B:CYS817 4.0 25.3 1.0 C2C B:HEM901 4.2 25.6 1.0 C3C B:HEM901 4.3 28.6 1.0 C3B B:HEM901 4.3 25.0 1.0 C3D B:HEM901 4.3 25.2 1.0 C2A B:HEM901 4.3 19.8 1.0 C3A B:HEM901 4.3 21.8 1.0 C2D B:HEM901 4.4 27.2 1.0 C2B B:HEM901 4.4 25.0 1.0 O B:ALA709 4.5 30.3 1.0 C B:CYS817 4.6 26.7 1.0 N B:LEU818 4.7 23.4 1.0 N B:GLY819 4.8 19.4 1.0 O B:HOH74 4.8 46.9 1.0

S.Y.Park, K.Yamane, S.Adachi, Y.Shiro, K.E.Weiss, S.A.Maves, S.G.Sligar. Thermophilic Cytochrome P450 (CYP119) From Sulfolobus Solfataricus: High Resolution Structure and Functional Properties. J.Inorg.Biochem. V. 91 491 2002.
ISSN: ISSN 0162-0134
PubMed: 12237217
DOI: 10.1107/S0907444900008234