Iron in PDB 2zqj: Substrate-Free Form of Cytochrome P450BSBETA

The structure of Substrate-Free Form of Cytochrome P450BSBETA, PDB code: 2zqj was solved by O.Shoji, T.Fujishiro, S.Nagano, T.Hirose, Y.Shiro, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.60 / 2.90
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	173.076, 173.076, 279.616, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 28.6

The binding sites of Iron atom in the Substrate-Free Form of Cytochrome P450BSBETA (pdb code 2zqj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Substrate-Free Form of Cytochrome P450BSBETA, PDB code: 2zqj:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Substrate-Free Form of Cytochrome P450BSBETA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Substrate-Free Form of Cytochrome P450BSBETA within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:24.7 occ:1.00 FE A:HEM501 0.0 24.7 1.0 ND A:HEM501 1.9 21.6 1.0 NA A:HEM501 1.9 23.2 1.0 NB A:HEM501 2.0 24.2 1.0 SG A:CYS363 2.2 28.2 1.0 NC A:HEM501 2.7 17.7 1.0 C4D A:HEM501 2.9 19.8 1.0 C1A A:HEM501 3.0 22.1 1.0 C1B A:HEM501 3.0 22.4 1.0 C4A A:HEM501 3.0 22.8 1.0 C1D A:HEM501 3.1 19.8 1.0 C4B A:HEM501 3.1 23.4 1.0 CHA A:HEM501 3.3 20.2 1.0 CB A:CYS363 3.3 26.8 1.0 CHB A:HEM501 3.4 21.8 1.0 C4C A:HEM501 3.6 19.1 1.0 C1C A:HEM501 3.6 21.1 1.0 CHD A:HEM501 3.6 17.8 1.0 CHC A:HEM501 3.7 21.8 1.0 CA A:CYS363 4.1 27.0 1.0 C2A A:HEM501 4.2 23.3 1.0 C3D A:HEM501 4.2 19.2 1.0 C3A A:HEM501 4.2 22.3 1.0 C2D A:HEM501 4.2 19.1 1.0 C2B A:HEM501 4.2 21.1 1.0 C3B A:HEM501 4.3 23.5 1.0 C3C A:HEM501 4.8 19.2 1.0 C2C A:HEM501 4.8 19.1 1.0 CD A:PRO364 5.0 27.8 1.0 NE2 A:GLN352 5.0 38.4 1.0

Iron binding site 2 out of 3 in the Substrate-Free Form of Cytochrome P450BSBETA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Substrate-Free Form of Cytochrome P450BSBETA within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:27.4 occ:1.00 FE B:HEM501 0.0 27.4 1.0 ND B:HEM501 1.9 25.9 1.0 NA B:HEM501 1.9 24.1 1.0 NB B:HEM501 2.0 26.0 1.0 SG B:CYS363 2.2 29.2 1.0 NC B:HEM501 2.7 24.0 1.0 C4A B:HEM501 2.9 25.1 1.0 C4D B:HEM501 2.9 25.8 1.0 C1B B:HEM501 2.9 24.1 1.0 C1A B:HEM501 3.0 23.7 1.0 C1D B:HEM501 3.1 24.4 1.0 C4B B:HEM501 3.1 25.8 1.0 CB B:CYS363 3.2 26.4 1.0 CHB B:HEM501 3.3 24.1 1.0 CHA B:HEM501 3.3 24.5 1.0 C4C B:HEM501 3.5 25.5 1.0 CHD B:HEM501 3.6 23.9 1.0 C1C B:HEM501 3.6 25.3 1.0 CHC B:HEM501 3.7 24.5 1.0 CA B:CYS363 4.0 26.4 1.0 C3A B:HEM501 4.2 24.5 1.0 C2A B:HEM501 4.2 24.4 1.0 C3D B:HEM501 4.2 25.4 1.0 C2B B:HEM501 4.2 24.4 1.0 C2D B:HEM501 4.2 24.6 1.0 C3B B:HEM501 4.3 23.6 1.0 C3C B:HEM501 4.8 25.8 1.0 C2C B:HEM501 4.8 26.2 1.0 C B:CYS363 4.8 26.1 1.0 N B:GLY365 4.9 23.9 1.0 CD B:PRO364 4.9 23.2 1.0 N B:PRO364 5.0 25.1 1.0

Iron binding site 3 out of 3 in the Substrate-Free Form of Cytochrome P450BSBETA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Substrate-Free Form of Cytochrome P450BSBETA within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:41.4 occ:1.00 FE C:HEM501 0.0 41.4 1.0 ND C:HEM501 1.9 40.9 1.0 NA C:HEM501 2.0 41.9 1.0 NB C:HEM501 2.0 40.8 1.0 SG C:CYS363 2.2 50.3 1.0 NC C:HEM501 2.7 41.6 1.0 C4D C:HEM501 2.9 41.2 1.0 C4A C:HEM501 3.0 40.3 1.0 C1A C:HEM501 3.0 41.2 1.0 C1B C:HEM501 3.0 39.3 1.0 C1D C:HEM501 3.0 42.0 1.0 C4B C:HEM501 3.2 39.3 1.0 CB C:CYS363 3.3 49.7 1.0 CHA C:HEM501 3.3 40.3 1.0 CHB C:HEM501 3.4 38.1 1.0 C4C C:HEM501 3.6 43.0 1.0 C1C C:HEM501 3.6 42.1 1.0 CHD C:HEM501 3.6 42.6 1.0 CHC C:HEM501 3.7 41.0 1.0 CA C:CYS363 4.1 48.6 1.0 C3D C:HEM501 4.2 41.3 1.0 C2D C:HEM501 4.2 41.4 1.0 C3A C:HEM501 4.2 40.3 1.0 C2A C:HEM501 4.2 40.5 1.0 C2B C:HEM501 4.3 39.1 1.0 C3B C:HEM501 4.4 38.5 1.0 NE2 C:GLN352 4.4 45.2 1.0 C3C C:HEM501 4.9 42.7 1.0 C2C C:HEM501 4.9 42.4 1.0 CD C:PRO364 4.9 46.1 1.0 C C:CYS363 4.9 48.0 1.0

O.Shoji, T.Fujishiro, S.Nagano, S.Tanaka, T.Hirose, Y.Shiro, Y.Watanabe. Understanding Substrate Misrecognition of Hydrogen Peroxide Dependent Cytochrome P450 From Bacillus Subtilis. J.Biol.Inorg.Chem. 2010.
ISSN: ESSN 1432-1327
PubMed: 20697922
DOI: 10.1007/S00775-010-0692-4