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Iron in PDB 5esg: Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole

Enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole

All present enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole:
1.14.13.70;

Protein crystallography data

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole, PDB code: 5esg 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) 33.66 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.240, 67.310, 80.830, 90.00, 98.65, 90.00
R / Rfree (%) 19.9 / 23.5

Other elements in 5esg:

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole (pdb code 5esg). 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) G73E Mutant Complexed with Itraconazole, PDB code: 5esg:

Iron binding site 1 out of 1 in 5esg

Go back to Iron Binding Sites List in 5esg
Iron binding site 1 out of 1 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) G73E Mutant Complexed with Itraconazole


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) G73E Mutant Complexed with Itraconazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe702

b:26.1
occ:1.00
 FE A:HEM702 0.0 26.1 1.0
NC A:HEM702 2.0 29.4 1.0
NA A:HEM702 2.0 29.3 1.0
NB A:HEM702 2.1 26.7 1.0
N39 A:1YN701 2.1 31.3 1.0
ND A:HEM702 2.1 25.3 1.0
SG A:CYS470 2.3 29.0 1.0
C1C A:HEM702 3.0 27.9 1.0
C4B A:HEM702 3.1 25.6 1.0
C1A A:HEM702 3.1 30.0 1.0
C4C A:HEM702 3.1 27.1 1.0
C4A A:HEM702 3.1 29.9 1.0
C1B A:HEM702 3.1 25.4 1.0
C4D A:HEM702 3.1 27.4 1.0
C40 A:1YN701 3.1 26.7 1.0
C38 A:1YN701 3.1 30.4 1.0
C1D A:HEM702 3.1 26.3 1.0
CB A:CYS470 3.3 25.7 1.0
CHC A:HEM702 3.4 28.4 1.0
CHA A:HEM702 3.4 25.8 1.0
CHB A:HEM702 3.5 24.0 1.0
CHD A:HEM702 3.5 25.4 1.0
CA A:CYS470 4.1 28.6 1.0
N37 A:1YN701 4.2 31.8 1.0
C2C A:HEM702 4.3 25.5 1.0
C3C A:HEM702 4.3 28.9 1.0
C3A A:HEM702 4.3 27.6 1.0
C2A A:HEM702 4.3 29.3 1.0
C3B A:HEM702 4.3 25.9 1.0
N41 A:1YN701 4.3 30.0 1.0
C2B A:HEM702 4.3 27.2 1.0
C3D A:HEM702 4.4 26.7 1.0
C2D A:HEM702 4.4 29.0 1.0
N A:GLY472 4.8 24.6 1.0
N A:ILE471 4.9 25.5 1.0
C A:CYS470 5.0 29.4 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: Tue Aug 6 00:31:50 2024

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