Iron in PDB 3ld6: Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Ketoconazole

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

The structure of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Ketoconazole, PDB code: 3ld6 was solved by N.Strushkevich, W.Tempel, F.Mackenzie, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, 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)	24.29 / 2.80
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	145.726, 145.726, 110.341, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 27.5

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

Chlorine

(Cl)

4 atoms

The binding sites of Iron atom in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Ketoconazole (pdb code 3ld6). 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 Ketoconazole, PDB code: 3ld6:
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 Ketoconazole


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 Ketoconazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:33.1 occ:1.00 FE A:HEM601 0.0 33.1 1.0 NC A:HEM601 2.0 32.6 1.0 ND A:HEM601 2.1 32.2 1.0 NB A:HEM601 2.1 33.1 1.0 NA A:HEM601 2.1 32.2 1.0 SG A:CYS449 2.4 36.8 1.0 N2 A:KKK602 2.4 39.5 1.0 C1 A:KKK602 2.9 42.0 1.0 C4C A:HEM601 3.0 32.3 1.0 C1C A:HEM601 3.0 32.8 1.0 C1D A:HEM601 3.0 31.8 1.0 C4D A:HEM601 3.1 32.1 1.0 C4B A:HEM601 3.1 33.1 1.0 C1B A:HEM601 3.1 32.0 1.0 C1A A:HEM601 3.1 32.7 1.0 C4A A:HEM601 3.1 32.1 1.0 CB A:CYS449 3.4 39.2 1.0 CHD A:HEM601 3.4 31.8 1.0 CHC A:HEM601 3.4 33.0 1.0 CHB A:HEM601 3.4 32.3 1.0 CHA A:HEM601 3.5 32.6 1.0 C2 A:KKK602 3.6 41.2 1.0 CA A:CYS449 4.2 39.5 1.0 N1 A:KKK602 4.2 42.9 1.0 C3C A:HEM601 4.2 32.4 1.0 C2C A:HEM601 4.2 32.1 1.0 C2D A:HEM601 4.3 32.1 1.0 C3D A:HEM601 4.3 32.1 1.0 C3B A:HEM601 4.3 33.2 1.0 C2B A:HEM601 4.3 32.1 1.0 C3A A:HEM601 4.3 32.2 1.0 C2A A:HEM601 4.3 32.6 1.0 C3 A:KKK602 4.6 42.0 1.0 N A:ILE450 4.9 39.0 1.0 N A:GLY451 4.9 38.4 1.0 CD1 A:ILE377 5.0 43.5 1.0

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


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 Ketoconazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:46.1 occ:1.00 FE B:HEM601 0.0 46.1 1.0 NC B:HEM601 2.0 45.4 1.0 NA B:HEM601 2.0 43.1 1.0 NB B:HEM601 2.1 43.5 1.0 ND B:HEM601 2.1 44.5 1.0 N2 B:KKK602 2.2 53.9 1.0 SG B:CYS449 2.4 47.1 1.0 C1 B:KKK602 2.9 54.7 1.0 C4C B:HEM601 3.0 45.8 1.0 C4A B:HEM601 3.0 42.3 1.0 C1B B:HEM601 3.1 42.6 1.0 C1C B:HEM601 3.1 46.3 1.0 C1A B:HEM601 3.1 42.8 1.0 C4B B:HEM601 3.1 44.1 1.0 C1D B:HEM601 3.1 44.2 1.0 C4D B:HEM601 3.2 44.5 1.0 CHD B:HEM601 3.4 45.4 1.0 CHB B:HEM601 3.4 41.4 1.0 C2 B:KKK602 3.4 54.7 1.0 CHC B:HEM601 3.5 45.7 1.0 CHA B:HEM601 3.5 43.9 1.0 CB B:CYS449 3.5 49.1 1.0 N1 B:KKK602 4.1 56.0 1.0 C3C B:HEM601 4.2 46.9 1.0 C2C B:HEM601 4.3 46.5 1.0 C3A B:HEM601 4.3 42.4 1.0 C2A B:HEM601 4.3 41.8 1.0 C2B B:HEM601 4.3 42.0 1.0 C3B B:HEM601 4.3 42.7 1.0 CA B:CYS449 4.3 49.5 1.0 C2D B:HEM601 4.4 44.0 1.0 C3 B:KKK602 4.4 55.0 1.0 C3D B:HEM601 4.4 44.1 1.0 N B:ILE450 4.9 48.9 1.0 N B:GLY451 4.9 48.2 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: ISSN 0022-2836
PubMed: 20149798
DOI: 10.1016/J.JMB.2010.01.075