Chlorine 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:

Iron

(Fe)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Cytochrome P450 2B37 From Desert Woodrat in Complex with 4-(4-Chlorophenyl)Imidazole, PDB code: 5e0e:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 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 Chlorine with other atoms in the Cl 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:Cl502 b:0.4 occ:1.00 CL A:CPZ502 0.0 0.4 1.0 C9 A:CPZ502 1.7 92.9 1.0 C10 A:CPZ502 2.7 90.2 1.0 C8 A:CPZ502 2.7 91.8 1.0 CD1 A:ILE101 3.0 67.7 1.0 C11 A:CPZ502 4.0 88.4 1.0 C7 A:CPZ502 4.0 89.6 1.0 N3 A:CPZ503 4.2 0.5 1.0 CE2 A:PHE297 4.2 73.8 1.0 CZ A:PHE115 4.4 73.2 1.0 CG1 A:ILE101 4.4 68.5 1.0 CG2 A:VAL367 4.4 66.6 1.0 C5 A:CPZ503 4.4 0.9 1.0 C4 A:CPZ503 4.4 0.7 1.0 C6 A:CPZ502 4.5 88.1 1.0 CD2 A:PHE297 4.7 71.7 1.0 C2 A:CPZ503 4.7 0.8 1.0 N1 A:CPZ503 4.7 0.2 1.0 CE2 A:PHE115 4.9 72.6 1.0 C6 A:CPZ503 5.0 0.3 1.0

Chlorine binding site 2 out of 3 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 Chlorine with other atoms in the Cl binding site number 2 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:Cl503 b:95.7 occ:1.00 CL A:CPZ503 0.0 95.7 1.0 C9 A:CPZ503 1.7 0.1 1.0 C10 A:CPZ503 2.7 0.3 1.0 C8 A:CPZ503 2.7 0.7 1.0 O A:HOH615 3.4 53.0 1.0 OH A:TYR389 3.9 68.7 1.0 C7 A:CPZ503 4.0 0.5 1.0 C11 A:CPZ503 4.0 0.6 1.0 CZ A:TYR389 4.4 68.7 1.0 CG A:GLU218 4.4 77.0 1.0 C6 A:CPZ503 4.5 0.3 1.0 CE2 A:TYR389 4.5 67.7 1.0 CD A:GLU218 4.8 76.6 1.0

Chlorine binding site 3 out of 3 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 Chlorine with other atoms in the Cl binding site number 3 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:Cl504 b:0.4 occ:1.00 CL A:CPZ504 0.0 0.4 1.0 C9 A:CPZ504 1.7 0.8 1.0 C10 A:CPZ504 2.7 1.0 1.0 C8 A:CPZ504 2.7 0.9 1.0 CA A:ASP47 3.6 0.4 1.0 O A:ASP47 3.7 0.6 1.0 CB A:ASP47 4.0 0.3 1.0 C11 A:CPZ504 4.0 0.2 1.0 C7 A:CPZ504 4.0 0.3 1.0 O A:GLY49 4.0 0.2 1.0 C A:ASP47 4.2 0.7 1.0 C6 A:CPZ504 4.5 0.8 1.0 N A:ASP47 4.7 0.4 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