Iron in PDB 7di3: Cytochrome P450 (CYP105D18) W.T.

The structure of Cytochrome P450 (CYP105D18) W.T., PDB code: 7di3 was solved by H.Do, J.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.42 / 1.69
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.688, 52.444, 87.952, 90, 110.82, 90
R / Rfree (%)	16.6 / 21.3

The binding sites of Iron atom in the Cytochrome P450 (CYP105D18) W.T. (pdb code 7di3). 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 P450 (CYP105D18) W.T., PDB code: 7di3:

Iron binding site 1 out of 1 in the Cytochrome P450 (CYP105D18) W.T.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 (CYP105D18) W.T. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:17.0 occ:1.00 FE A:HEM401 0.0 17.0 1.0 NA A:HEM401 2.0 14.1 1.0 ND A:HEM401 2.0 16.2 1.0 NC A:HEM401 2.1 16.3 1.0 NB A:HEM401 2.1 14.7 1.0 O A:HOH574 2.2 30.1 1.0 SG A:CYS345 2.3 16.4 1.0 C4B A:HEM401 3.0 15.9 1.0 C4D A:HEM401 3.0 17.4 1.0 C1A A:HEM401 3.0 14.8 1.0 C1D A:HEM401 3.0 17.2 1.0 C4A A:HEM401 3.0 13.9 1.0 C1B A:HEM401 3.1 14.2 1.0 C1C A:HEM401 3.1 17.2 1.0 C4C A:HEM401 3.1 16.1 1.0 CB A:CYS345 3.4 16.2 1.0 CHA A:HEM401 3.4 14.7 1.0 CHC A:HEM401 3.4 17.8 1.0 CHB A:HEM401 3.5 12.8 1.0 CHD A:HEM401 3.5 16.6 1.0 CA A:CYS345 3.9 15.1 1.0 O A:ALA235 4.1 19.8 1.0 C2A A:HEM401 4.2 14.2 1.0 C3B A:HEM401 4.2 15.4 1.0 C3A A:HEM401 4.2 14.3 1.0 C2D A:HEM401 4.3 17.9 1.0 C3C A:HEM401 4.3 19.2 1.0 C2C A:HEM401 4.3 18.0 1.0 C2B A:HEM401 4.3 15.2 1.0 C3D A:HEM401 4.3 17.0 1.0 C A:CYS345 4.7 14.2 1.0 N A:GLY347 4.8 19.1 1.0 N A:LEU346 4.8 15.4 1.0 CB A:ALA235 4.8 19.6 1.0 C A:ALA235 4.9 17.9 1.0

B.D.Pardhe, H.Do, C.S.Jeong, K.H.Kim, J.H.Lee, T.J.Oh. Characterization of High-H2O2-Tolerant Bacterial Cytochrome P450 CYP105D18: Insights Into Papaverine N-Oxidation. Iucrj 684 2021.
ISSN: ESSN 2052-2525
DOI: 10.1107/S2052252521005522