Iron in PDB 1io7: 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: 1io7 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)	80.00 / 1.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.194, 86.194, 221.597, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 26.7

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 1io7). 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: 1io7:
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:Fe1401 b:10.2 occ:1.00 FE A:HEM1401 0.0 10.2 1.0 NA A:HEM1401 2.0 9.6 1.0 NC A:HEM1401 2.0 11.7 1.0 ND A:HEM1401 2.0 10.8 1.0 NB A:HEM1401 2.0 10.3 1.0 SG A:CYS317 2.3 12.8 1.0 O A:HOH1402 2.3 16.9 1.0 C4A A:HEM1401 3.0 9.2 1.0 C4D A:HEM1401 3.0 8.9 1.0 C1C A:HEM1401 3.1 10.8 1.0 C4C A:HEM1401 3.1 11.0 1.0 C4B A:HEM1401 3.1 9.2 1.0 C1D A:HEM1401 3.1 10.9 1.0 C1B A:HEM1401 3.1 7.9 1.0 C1A A:HEM1401 3.1 9.2 1.0 CB A:CYS317 3.4 10.9 1.0 CHC A:HEM1401 3.4 9.9 1.0 CHB A:HEM1401 3.4 8.1 1.0 CHD A:HEM1401 3.4 11.5 1.0 CHA A:HEM1401 3.4 9.5 1.0 CA A:CYS317 4.1 10.5 1.0 O A:HOH1462 4.2 24.1 1.0 C3A A:HEM1401 4.3 9.4 1.0 C3D A:HEM1401 4.3 9.7 1.0 C3C A:HEM1401 4.3 13.4 1.0 C2A A:HEM1401 4.3 10.6 1.0 C2C A:HEM1401 4.3 12.4 1.0 C2D A:HEM1401 4.3 10.6 1.0 C3B A:HEM1401 4.3 10.3 1.0 C2B A:HEM1401 4.3 9.3 1.0 O A:ALA209 4.5 13.2 1.0 N A:GLY319 4.7 12.8 1.0 C A:CYS317 4.8 10.7 1.0 N A:LEU318 4.8 10.2 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:10.8 occ:1.00 FE B:HEM901 0.0 10.8 1.0 O B:HOH902 1.9 23.0 1.0 NB B:HEM901 2.0 8.2 1.0 NC B:HEM901 2.0 9.2 1.0 NA B:HEM901 2.0 8.4 1.0 ND B:HEM901 2.0 9.9 1.0 SG B:CYS817 2.4 12.3 1.0 C4B B:HEM901 3.0 8.0 1.0 C1B B:HEM901 3.0 9.2 1.0 C1C B:HEM901 3.0 9.7 1.0 C1D B:HEM901 3.0 10.7 1.0 C4C B:HEM901 3.0 10.4 1.0 C4D B:HEM901 3.1 9.4 1.0 C4A B:HEM901 3.1 8.2 1.0 C1A B:HEM901 3.1 9.3 1.0 CHC B:HEM901 3.4 9.8 1.0 CHD B:HEM901 3.4 9.8 1.0 CHB B:HEM901 3.4 8.4 1.0 CHA B:HEM901 3.5 8.5 1.0 CB B:CYS817 3.5 10.4 1.0 CA B:CYS817 4.2 10.7 1.0 C3D B:HEM901 4.3 9.7 1.0 C3B B:HEM901 4.3 10.1 1.0 C2D B:HEM901 4.3 9.9 1.0 C2B B:HEM901 4.3 7.7 1.0 C2A B:HEM901 4.3 10.9 1.0 C3C B:HEM901 4.3 13.3 1.0 C3A B:HEM901 4.3 9.5 1.0 C2C B:HEM901 4.3 9.1 1.0 O B:HOH387 4.3 42.0 1.0 O B:ALA709 4.6 13.9 1.0 N B:GLY819 4.7 10.8 1.0 N B:LEU818 4.8 13.6 1.0 C B:CYS817 4.8 9.3 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