Iron in PDB 5e0e: Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole

The structure of Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole, PDB code: 5e0e was solved by M.B.Shah, J.R.Halpert, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.36 / 3.40
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	144.770, 144.770, 104.470, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 29

The structure of Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole (pdb code 5e0e). 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 Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole, PDB code: 5e0e:

Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:58.9 occ:1.00 FE A:HEM501 0.0 58.9 1.0 N1 A:CPZ502 1.6 85.1 1.0 SG A:CYS436 2.0 67.7 1.0 NB A:HEM501 2.0 61.0 1.0 NC A:HEM501 2.0 58.2 1.0 NA A:HEM501 2.0 58.6 1.0 ND A:HEM501 2.1 59.0 1.0 C5 A:CPZ502 2.7 86.8 1.0 C2 A:CPZ502 2.7 85.7 1.0 C4C A:HEM501 3.0 57.9 1.0 C1B A:HEM501 3.0 62.2 1.0 C4A A:HEM501 3.0 59.3 1.0 C1C A:HEM501 3.0 58.0 1.0 C1D A:HEM501 3.0 58.1 1.0 C4B A:HEM501 3.1 62.3 1.0 C1A A:HEM501 3.2 58.9 1.0 C4D A:HEM501 3.2 59.0 1.0 CHD A:HEM501 3.3 57.8 1.0 CHB A:HEM501 3.3 61.5 1.0 CB A:CYS436 3.4 70.3 1.0 CHC A:HEM501 3.4 60.8 1.0 CHA A:HEM501 3.6 59.3 1.0 N3 A:CPZ502 3.8 87.2 1.0 C4 A:CPZ502 3.8 86.9 1.0 CA A:CYS436 4.1 70.3 1.0 C3C A:HEM501 4.2 57.1 1.0 C2B A:HEM501 4.2 62.2 1.0 C3A A:HEM501 4.2 59.2 1.0 C2C A:HEM501 4.2 57.0 1.0 C3B A:HEM501 4.3 63.0 1.0 C2A A:HEM501 4.3 59.2 1.0 C2D A:HEM501 4.3 58.0 1.0 C3D A:HEM501 4.4 58.7 1.0 O A:GLY438 4.7 78.8 1.0 CB A:ALA298 4.7 67.4 1.0 C A:CYS436 4.8 70.4 1.0 CD1 A:PHE429 4.8 82.2 1.0 N A:LEU437 4.8 70.8 1.0

M.B.Shah, J.Liu, L.Huo, Q.Zhang, M.D.Dearing, P.R.Wilderman, G.D.Szklarz, C.D.Stout, J.R.Halpert. Structure-Function Analysis of Mammalian CYP2B Enzymes Using 7-Substituted Coumarin Derivatives As Probes: Utility of Crystal Structures and Molecular Modeling in Understanding Xenobiotic Metabolism. Mol.Pharmacol. V. 89 435 2016.
ISSN: ESSN 1521-0111
PubMed: 26826176
DOI: 10.1124/MOL.115.102111