Iron in PDB 5xjn: Cytochrome P450 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate

The structure of Cytochrome P450 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate, PDB code: 5xjn was solved by S.Dong, L.Du, S.Li, Y.Feng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.45 / 1.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.070, 86.070, 125.040, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 20.9

The binding sites of Iron atom in the Cytochrome P450 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate (pdb code 5xjn). 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 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate, PDB code: 5xjn:

Iron binding site 1 out of 1 in the Cytochrome P450 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 Crej in Complex with (4-Ethylphenyl) Dihydrogen Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:10.9 occ:1.00 FE A:HEM502 0.0 10.9 1.0 NB A:HEM502 2.0 11.0 1.0 NA A:HEM502 2.1 10.7 1.0 NC A:HEM502 2.1 12.5 1.0 ND A:HEM502 2.1 8.4 1.0 SG A:CYS376 2.4 11.7 1.0 C4B A:HEM502 3.0 7.8 1.0 C1C A:HEM502 3.0 11.1 1.0 C1B A:HEM502 3.1 8.9 1.0 C1A A:HEM502 3.1 8.4 1.0 C1D A:HEM502 3.1 9.1 1.0 C4A A:HEM502 3.1 7.5 1.0 C4D A:HEM502 3.1 7.0 1.0 C4C A:HEM502 3.1 10.2 1.0 HB2 A:CYS376 3.2 14.8 1.0 H112 A:88L501 3.2 16.5 1.0 CB A:CYS376 3.3 12.3 1.0 CHC A:HEM502 3.4 8.9 1.0 HA A:CYS376 3.4 14.1 1.0 CHA A:HEM502 3.4 10.5 1.0 CHD A:HEM502 3.5 10.0 1.0 CHB A:HEM502 3.5 9.7 1.0 H111 A:88L501 3.5 16.5 1.0 C11 A:88L501 3.8 13.7 1.0 H A:GLY378 3.9 14.9 1.0 CA A:CYS376 3.9 11.8 1.0 HB1 A:ALA265 4.0 16.6 1.0 H A:LEU377 4.0 13.7 1.0 HB3 A:CYS376 4.2 14.8 1.0 H081 A:88L501 4.2 12.3 1.0 HD1 A:PHE369 4.3 12.9 1.0 C2C A:HEM502 4.3 10.6 1.0 C3B A:HEM502 4.3 8.2 1.0 C3C A:HEM502 4.3 12.6 1.0 C2B A:HEM502 4.3 10.1 1.0 C2D A:HEM502 4.3 10.4 1.0 C3A A:HEM502 4.3 8.7 1.0 C2A A:HEM502 4.3 10.5 1.0 C3D A:HEM502 4.3 11.5 1.0 H102 A:88L501 4.3 14.6 1.0 HG1 A:THR269 4.3 20.0 1.0 HHC A:HEM502 4.4 10.6 1.0 HHA A:HEM502 4.4 12.6 1.0 HHB A:HEM502 4.4 11.7 1.0 HHD A:HEM502 4.4 12.0 1.0 N A:LEU377 4.5 11.4 1.0 H113 A:88L501 4.5 16.5 1.0 C A:CYS376 4.6 12.1 1.0 C10 A:88L501 4.6 12.2 1.0 N A:GLY378 4.8 12.4 1.0 CB A:ALA265 4.9 13.8 1.0 C08 A:88L501 5.0 10.3 1.0

L.Du, S.Dong, X.Zhang, C.Jiang, J.Chen, L.Yao, X.Wang, X.Wan, X.Liu, X.Wang, S.Huang, Q.Cui, Y.Feng, S.J.Liu, S.Li. Selective Oxidation of Aliphatic C-H Bonds in Alkylphenols By A Chemomimetic Biocatalytic System Proc. Natl. Acad. Sci. V. 114 E5129 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28607077
DOI: 10.1073/PNAS.1702317114