Iron in PDB 3jus: Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole

All present enzymatic activity of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole:
1.14.13.70;

The structure of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole, PDB code: 3jus was solved by N.Strushkevich, F.Mackenzie, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, S.A.Usanov, H.Park, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.52 / 2.90
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	146.626, 146.626, 110.560, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 27.2

The structure of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole also contains other interesting chemical elements:

Chlorine

(Cl)

12 atoms

The binding sites of Iron atom in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole (pdb code 3jus). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole, PDB code: 3jus:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole


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 Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:46.5 occ:1.00 FE A:HEM601 0.0 46.5 1.0 NC A:HEM601 2.0 47.4 1.0 NB A:HEM601 2.0 47.1 1.0 NA A:HEM601 2.1 47.9 1.0 ND A:HEM601 2.1 47.1 1.0 N19 A:ECL600 2.2 60.8 0.5 N19 A:ECN602 2.3 54.0 0.5 SG A:CYS449 2.4 51.6 1.0 C1C A:HEM601 3.0 47.9 1.0 C4B A:HEM601 3.0 46.9 1.0 C4C A:HEM601 3.0 47.6 1.0 C1A A:HEM601 3.1 48.9 1.0 C3 A:ECL600 3.1 61.8 0.5 C1B A:HEM601 3.1 47.1 1.0 C4D A:HEM601 3.1 47.6 1.0 C1D A:HEM601 3.1 46.9 1.0 C4A A:HEM601 3.1 47.9 1.0 C6 A:ECL600 3.2 61.4 0.5 C3 A:ECN602 3.2 55.2 0.5 C6 A:ECN602 3.3 54.7 0.5 CB A:CYS449 3.3 52.7 1.0 CHC A:HEM601 3.4 47.8 1.0 CHD A:HEM601 3.4 48.3 1.0 CHA A:HEM601 3.4 48.7 1.0 CHB A:HEM601 3.5 47.5 1.0 CA A:CYS449 4.1 53.0 1.0 N1 A:ECL600 4.2 62.7 0.5 C3C A:HEM601 4.2 47.4 1.0 C2C A:HEM601 4.2 48.0 1.0 C7 A:ECL600 4.3 62.4 0.5 C3B A:HEM601 4.3 46.6 1.0 C2B A:HEM601 4.3 47.0 1.0 C2A A:HEM601 4.3 49.0 1.0 N1 A:ECN602 4.3 56.1 0.5 C3A A:HEM601 4.3 47.4 1.0 C3D A:HEM601 4.3 47.6 1.0 C2D A:HEM601 4.4 47.3 1.0 C7 A:ECN602 4.4 55.9 0.5 N A:ILE450 4.9 52.3 1.0 CD1 A:ILE377 4.9 52.7 1.0 C8 A:ECN602 4.9 58.3 0.5 C10 A:ECN602 5.0 59.0 0.5 N A:GLY451 5.0 52.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:52.4 occ:1.00 FE B:HEM601 0.0 52.4 1.0 NC B:HEM601 2.0 51.0 1.0 NB B:HEM601 2.0 50.9 1.0 NA B:HEM601 2.1 50.9 1.0 N19 B:ECL600 2.1 66.7 0.5 ND B:HEM601 2.1 51.1 1.0 N19 B:ECN602 2.2 74.9 0.5 SG B:CYS449 2.4 58.3 1.0 C3 B:ECN602 3.0 75.0 0.5 C3 B:ECL600 3.0 66.8 0.5 C1C B:HEM601 3.0 51.3 1.0 C4B B:HEM601 3.0 51.4 1.0 C4C B:HEM601 3.0 50.8 1.0 C1A B:HEM601 3.1 51.5 1.0 C1B B:HEM601 3.1 50.6 1.0 C4D B:HEM601 3.1 51.6 1.0 C4A B:HEM601 3.1 51.1 1.0 C1D B:HEM601 3.1 51.0 1.0 C6 B:ECL600 3.1 66.7 0.5 C6 B:ECN602 3.2 74.9 0.5 CHC B:HEM601 3.4 51.6 1.0 CHA B:HEM601 3.4 52.3 1.0 CHD B:HEM601 3.4 50.8 1.0 CHB B:HEM601 3.5 50.4 1.0 CB B:CYS449 3.5 59.0 1.0 CA B:CYS449 4.1 59.2 1.0 N1 B:ECN602 4.1 75.5 0.5 N1 B:ECL600 4.2 67.4 0.5 C7 B:ECL600 4.2 67.1 0.5 C3C B:HEM601 4.3 51.0 1.0 C2C B:HEM601 4.3 50.8 1.0 C7 B:ECN602 4.3 75.2 0.5 C3B B:HEM601 4.3 51.7 1.0 C2B B:HEM601 4.3 50.6 1.0 C2A B:HEM601 4.3 51.5 1.0 C3A B:HEM601 4.3 51.5 1.0 C2D B:HEM601 4.3 51.0 1.0 C3D B:HEM601 4.3 50.5 1.0 N B:ILE450 4.7 58.9 1.0 CD1 B:ILE377 4.7 57.9 1.0 C8 B:ECN602 4.8 78.1 0.5 N B:GLY451 4.9 58.7 1.0 C B:CYS449 5.0 59.1 1.0

N.Strushkevich, S.A.Usanov, H.W.Park. Structural Basis of Human CYP51 Inhibition By Antifungal Azoles. J. Mol. Biol. V. 397 1067 2010.
ISSN: ESSN 1089-8638
PubMed: 20149798
DOI: 10.1016/J.JMB.2010.01.075