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Iron in PDB 5ese: Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole

Enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole

All present enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole:
1.14.13.70;

Protein crystallography data

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole, PDB code: 5ese was solved by A.Sagatova, M.V.Keniya, R.K.Wilson, M.Sabherwal, J.D.A.Tyndall, B.C.Monk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.49 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.350, 67.280, 81.020, 90.00, 99.24, 90.00
R / Rfree (%) 21 / 23.8

Other elements in 5ese:

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole (pdb code 5ese). 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 Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole, PDB code: 5ese:

Iron binding site 1 out of 1 in 5ese

Go back to Iron Binding Sites List in 5ese
Iron binding site 1 out of 1 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73R Mutant Complexed with Fluconazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:29.3
occ:1.00
 FE A:HEM601 0.0 29.3 1.0
NC A:HEM601 2.0 38.2 1.0
NB A:HEM601 2.0 39.6 1.0
NA A:HEM601 2.1 40.7 1.0
ND A:HEM601 2.1 38.9 1.0
N5 A:TPF602 2.1 47.2 1.0
SG A:CYS470 2.3 37.7 1.0
C7 A:TPF602 2.9 36.2 1.0
C1C A:HEM601 3.0 41.2 1.0
C4B A:HEM601 3.0 32.7 1.0
C4C A:HEM601 3.1 40.8 1.0
C4A A:HEM601 3.1 41.9 1.0
C1B A:HEM601 3.1 34.3 1.0
C1A A:HEM601 3.1 43.9 1.0
C1D A:HEM601 3.1 37.5 1.0
C4D A:HEM601 3.1 36.9 1.0
C6 A:TPF602 3.3 42.8 1.0
CB A:CYS470 3.3 41.5 1.0
CHC A:HEM601 3.4 42.1 1.0
CHD A:HEM601 3.4 38.3 1.0
CHB A:HEM601 3.4 36.4 1.0
CHA A:HEM601 3.5 37.7 1.0
CA A:CYS470 4.1 40.6 1.0
N6 A:TPF602 4.1 36.9 1.0
C2C A:HEM601 4.2 40.6 1.0
N4 A:TPF602 4.3 41.0 1.0
C3C A:HEM601 4.3 42.1 1.0
C3B A:HEM601 4.3 38.8 1.0
C2B A:HEM601 4.3 44.4 1.0
C3A A:HEM601 4.3 38.0 1.0
C2A A:HEM601 4.3 41.4 1.0
C2D A:HEM601 4.3 45.7 1.0
C3D A:HEM601 4.3 43.6 1.0
N A:GLY472 4.8 39.5 1.0
N A:ILE471 4.9 37.7 1.0

Reference:

A.Sagatova, M.V.Keniya, R.K.Wilson, M.Sabherwal, J.D.A.Tyndall, B.C.Monk. Structures of Lanosterol 14-Alpha Demethylase Mutants. To Be Published.
Page generated: Sun Dec 13 16:00:46 2020

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