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Iron in PDB 5esn: Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure

Enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure

All present enzymatic activity of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure:
1.14.13.70;

Protein crystallography data

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure, PDB code: 5esn 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) 38.30 / 2.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.520, 65.950, 80.950, 90.00, 98.84, 90.00
R / Rfree (%) 18.4 / 22.8

Iron Binding Sites:

The binding sites of Iron atom in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure (pdb code 5esn). 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) T322I Mutant Structure, PDB code: 5esn:

Iron binding site 1 out of 1 in 5esn

Go back to Iron Binding Sites List in 5esn
Iron binding site 1 out of 1 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) T322I Mutant Structure


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) T322I Mutant Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:32.7
occ:1.00
FE A:HEM601 0.0 32.7 1.0
NC A:HEM601 2.0 33.0 1.0
NB A:HEM601 2.0 29.0 1.0
ND A:HEM601 2.1 28.5 1.0
NA A:HEM601 2.1 30.1 1.0
SG A:CYS470 2.3 34.6 1.0
C4C A:HEM601 3.0 31.0 1.0
C1D A:HEM601 3.0 28.2 1.0
C1B A:HEM601 3.1 30.4 1.0
C4A A:HEM601 3.1 28.9 1.0
C1C A:HEM601 3.1 31.8 1.0
C4B A:HEM601 3.1 27.4 1.0
C4D A:HEM601 3.1 30.5 1.0
C1A A:HEM601 3.1 31.4 1.0
CB A:CYS470 3.3 30.9 1.0
CHD A:HEM601 3.4 28.6 1.0
CHB A:HEM601 3.4 29.5 1.0
CHC A:HEM601 3.5 30.7 1.0
CHA A:HEM601 3.5 28.7 1.0
CA A:CYS470 4.1 35.5 1.0
C3C A:HEM601 4.2 31.6 1.0
C2D A:HEM601 4.2 36.2 1.0
C2C A:HEM601 4.3 30.2 1.0
C3D A:HEM601 4.3 35.6 1.0
C2B A:HEM601 4.3 33.7 1.0
C3B A:HEM601 4.3 30.6 1.0
C3A A:HEM601 4.3 33.2 1.0
C2A A:HEM601 4.3 33.2 1.0
O A:GLY314 4.4 40.0 1.0
N A:GLY472 4.8 32.4 1.0
N A:ILE471 4.9 32.9 1.0
C A:CYS470 5.0 37.5 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 00:33:28 2024

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