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Iron in PDB 4lxj: Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound

Enzymatic activity of Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound

All present enzymatic activity of Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound:
1.14.13.70;

Protein crystallography data

The structure of Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound, PDB code: 4lxj was solved by B.C.Monk, T.M.Tomasiak, M.V.Keniya, F.U.Huschmann, J.D.A.Tyndall, J.D.O'connell Iii, R.D.Cannon, J.Mcdonald, A.Rodriguez, J.Finer-Moore, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.33 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.213, 67.005, 80.378, 90.00, 99.54, 90.00
R / Rfree (%) 19.5 / 22.7

Iron Binding Sites:

The binding sites of Iron atom in the Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound (pdb code 4lxj). 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 Lanosterol 14-Alpha Demethylase with Lanosterol Bound, PDB code: 4lxj:

Iron binding site 1 out of 1 in 4lxj

Go back to Iron Binding Sites List in 4lxj
Iron binding site 1 out of 1 in the Saccharomyces Cerevisiae Lanosterol 14-Alpha Demethylase with Lanosterol Bound


Mono view


Stereo pair view

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

b:35.1
occ:1.00
FE A:HEM601 0.0 35.1 1.0
NA A:HEM601 2.0 36.6 1.0
NC A:HEM601 2.0 36.5 1.0
NB A:HEM601 2.0 32.5 1.0
ND A:HEM601 2.1 30.5 1.0
SG A:CYS470 2.2 35.1 1.0
O1 A:OXY603 2.4 43.6 1.0
C1C A:HEM601 3.0 35.6 1.0
C4A A:HEM601 3.0 35.7 1.0
C4B A:HEM601 3.0 34.2 1.0
C1B A:HEM601 3.1 33.4 1.0
C4D A:HEM601 3.1 33.4 1.0
C4C A:HEM601 3.1 35.5 1.0
C1D A:HEM601 3.1 33.9 1.0
C1A A:HEM601 3.1 36.0 1.0
O2 A:OXY603 3.2 51.8 1.0
CB A:CYS470 3.3 32.9 1.0
CHC A:HEM601 3.4 35.6 1.0
CHB A:HEM601 3.4 33.5 1.0
CHD A:HEM601 3.5 33.5 1.0
CHA A:HEM601 3.5 34.1 1.0
CA A:CYS470 4.0 34.8 1.0
C2C A:HEM601 4.2 34.3 1.0
C3A A:HEM601 4.3 37.4 1.0
C3C A:HEM601 4.3 38.4 1.0
C3B A:HEM601 4.3 33.7 1.0
C2B A:HEM601 4.3 33.7 1.0
C3D A:HEM601 4.3 36.4 1.0
C2A A:HEM601 4.3 33.7 1.0
C2D A:HEM601 4.3 35.8 1.0
O A:GLY314 4.3 39.5 1.0
N A:GLY472 4.8 33.0 1.0
N A:ILE471 4.9 29.7 1.0
C A:CYS470 4.9 34.7 1.0

Reference:

B.C.Monk, T.M.Tomasiak, M.V.Keniya, F.U.Huschmann, J.D.Tyndall, J.D.O'connell, R.D.Cannon, J.G.Mcdonald, A.Rodriguez, J.S.Finer-Moore, R.M.Stroud. Architecture of A Single Membrane Spanning Cytochrome P450 Suggests Constraints That Orient the Catalytic Domain Relative to A Bilayer. Proc.Natl.Acad.Sci.Usa V. 111 3865 2014.
ISSN: ISSN 0027-8424
PubMed: 24613931
DOI: 10.1073/PNAS.1324245111
Page generated: Mon Aug 5 06:29:10 2024

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