Iron in PDB 3vno: Cytochrome P450SP Alpha (CYP152B1) Mutant R241E

All present enzymatic activity of Cytochrome P450SP Alpha (CYP152B1) Mutant R241E:
1.11.2.4;

The structure of Cytochrome P450SP Alpha (CYP152B1) Mutant R241E, PDB code: 3vno was solved by T.Fujishiro, O.Shoji, H.Sugimoto, Y.Shiro, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.79 / 2.17
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.539, 94.539, 113.004, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 22.7

The binding sites of Iron atom in the Cytochrome P450SP Alpha (CYP152B1) Mutant R241E (pdb code 3vno). 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 Cytochrome P450SP Alpha (CYP152B1) Mutant R241E, PDB code: 3vno:

Iron binding site 1 out of 1 in the Cytochrome P450SP Alpha (CYP152B1) Mutant R241E


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450SP Alpha (CYP152B1) Mutant R241E within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:2.3 occ:1.00 FE A:HEM501 0.0 2.3 1.0 NC A:HEM501 2.1 2.0 1.0 NA A:HEM501 2.1 2.0 1.0 ND A:HEM501 2.1 2.0 1.0 NB A:HEM501 2.1 2.0 1.0 SG A:CYS361 2.3 15.7 1.0 O A:HOH676 2.8 33.3 1.0 C1C A:HEM501 3.0 2.0 1.0 C1A A:HEM501 3.1 2.0 1.0 C4B A:HEM501 3.1 2.0 1.0 C4D A:HEM501 3.1 2.0 1.0 C1D A:HEM501 3.1 2.0 1.0 C4C A:HEM501 3.1 2.0 1.0 C1B A:HEM501 3.1 2.0 1.0 C4A A:HEM501 3.1 2.0 1.0 CB A:CYS361 3.4 11.8 1.0 CHC A:HEM501 3.4 2.0 1.0 CHD A:HEM501 3.4 2.0 1.0 CHA A:HEM501 3.4 2.0 1.0 CHB A:HEM501 3.5 2.0 1.0 CA A:CYS361 4.2 11.6 1.0 NE2 A:GLN350 4.3 15.0 1.0 C2C A:HEM501 4.3 2.0 1.0 C3B A:HEM501 4.3 2.0 1.0 C2A A:HEM501 4.3 2.0 1.0 C3C A:HEM501 4.3 2.0 1.0 C2B A:HEM501 4.3 2.0 1.0 C3A A:HEM501 4.3 2.0 1.0 C3D A:HEM501 4.3 2.0 1.0 C2D A:HEM501 4.3 2.0 1.0 O A:HOH679 4.5 36.9 1.0 CB A:PRO242 4.7 11.8 1.0 N A:GLY363 4.9 11.0 1.0 CD A:PRO362 4.9 10.1 1.0 C A:CYS361 5.0 10.5 1.0

O.Shoji, T.Fujishiro, K.Nishio, Y.Kano, H.Kimoto, S.-C.Chien, H.Onoda, A.Muramatsu, S.Tanaka, A.Hori, H.Sugimoto, Y.Shiro, Y.Watanabe. A Substrate-Binding-State Mimic of H2O2-Dependent Cytochrome P450 Produced By One-Point Mutagenesis and Peroxygenation of Non-Native Substrates Catalysis Science and V. 6 5806 2016TECHNOLOGY.
ISSN: ISSN 2044-4753
DOI: 10.1039/C6CY00630B