Iron in PDB 1ehg: Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S

The structure of Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S, PDB code: 1ehg was solved by H.Shimizu, S.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.751, 81.860, 85.720, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.3

The binding sites of Iron atom in the Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S (pdb code 1ehg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S, PDB code: 1ehg:

Iron binding site 1 out of 1 in the Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286 Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:6.6 occ:1.00 FE A:HEM501 0.0 6.6 1.0 NC A:HEM501 2.0 6.7 1.0 NA A:HEM501 2.0 4.9 1.0 NB A:HEM501 2.0 4.5 1.0 ND A:HEM501 2.0 4.4 1.0 SG A:CYS352 2.3 6.8 1.0 C1D A:HEM501 3.1 6.6 1.0 C4B A:HEM501 3.1 6.6 1.0 C1C A:HEM501 3.1 7.0 1.0 C4A A:HEM501 3.1 3.8 1.0 C4C A:HEM501 3.1 7.7 1.0 C1A A:HEM501 3.1 4.3 1.0 C4D A:HEM501 3.1 5.7 1.0 C1B A:HEM501 3.1 6.3 1.0 CB A:CYS352 3.4 4.3 1.0 O A:HOH873 3.4 29.0 1.0 CHC A:HEM501 3.4 6.7 1.0 CHD A:HEM501 3.4 6.7 1.0 CHA A:HEM501 3.5 5.4 1.0 CHB A:HEM501 3.5 6.4 1.0 CA A:CYS352 4.1 4.9 1.0 C2C A:HEM501 4.3 6.8 1.0 C3A A:HEM501 4.3 4.3 1.0 C3C A:HEM501 4.3 7.3 1.0 C2A A:HEM501 4.3 4.9 1.0 C2D A:HEM501 4.3 7.2 1.0 C3B A:HEM501 4.3 7.0 1.0 C3D A:HEM501 4.3 5.8 1.0 C2B A:HEM501 4.3 6.2 1.0 O A:HOH689 4.7 16.7 1.0 C A:CYS352 4.9 4.5 1.0 CA A:GLY240 5.0 6.9 1.0 CD1 A:PHE345 5.0 5.3 1.0 O A:ALA239 5.0 8.4 1.0 N A:ILE353 5.0 5.7 1.0

H.Shimizu, S.Park, D.Lee, H.Shoun, Y.Shiro. Crystal Structures of Cytochrome P450NOR and Its Mutants (SER286-->Val, Thr) in the Ferric Resting State at Cryogenic Temperature: A Comparative Analysis with Monooxygenase Cytochrome P450S. J.Inorg.Biochem. V. 81 191 2000.
ISSN: ISSN 0162-0134
PubMed: 11051564
DOI: 10.1016/S0162-0134(00)00103-3