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

Enzymatic activity of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole

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

Protein crystallography data

The structure of Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole, PDB code: 3jus was solved by N.Strushkevich, F.Mackenzie, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, S.A.Usanov, 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) 24.52 / 2.90
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 146.626, 146.626, 110.560, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 27.2

Other elements in 3jus:

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

Chlorine (Cl) 12 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole (pdb code 3jus). 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 Econazole, PDB code: 3jus:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3jus

Go back to Iron Binding Sites List in 3jus
Iron binding site 1 out of 2 in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole


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 Econazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:46.5
occ:1.00
FE A:HEM601 0.0 46.5 1.0
NC A:HEM601 2.0 47.4 1.0
NB A:HEM601 2.0 47.1 1.0
NA A:HEM601 2.1 47.9 1.0
ND A:HEM601 2.1 47.1 1.0
N19 A:ECL600 2.2 60.8 0.5
N19 A:ECN602 2.3 54.0 0.5
SG A:CYS449 2.4 51.6 1.0
C1C A:HEM601 3.0 47.9 1.0
C4B A:HEM601 3.0 46.9 1.0
C4C A:HEM601 3.0 47.6 1.0
C1A A:HEM601 3.1 48.9 1.0
C3 A:ECL600 3.1 61.8 0.5
C1B A:HEM601 3.1 47.1 1.0
C4D A:HEM601 3.1 47.6 1.0
C1D A:HEM601 3.1 46.9 1.0
C4A A:HEM601 3.1 47.9 1.0
C6 A:ECL600 3.2 61.4 0.5
C3 A:ECN602 3.2 55.2 0.5
C6 A:ECN602 3.3 54.7 0.5
CB A:CYS449 3.3 52.7 1.0
CHC A:HEM601 3.4 47.8 1.0
CHD A:HEM601 3.4 48.3 1.0
CHA A:HEM601 3.4 48.7 1.0
CHB A:HEM601 3.5 47.5 1.0
CA A:CYS449 4.1 53.0 1.0
N1 A:ECL600 4.2 62.7 0.5
C3C A:HEM601 4.2 47.4 1.0
C2C A:HEM601 4.2 48.0 1.0
C7 A:ECL600 4.3 62.4 0.5
C3B A:HEM601 4.3 46.6 1.0
C2B A:HEM601 4.3 47.0 1.0
C2A A:HEM601 4.3 49.0 1.0
N1 A:ECN602 4.3 56.1 0.5
C3A A:HEM601 4.3 47.4 1.0
C3D A:HEM601 4.3 47.6 1.0
C2D A:HEM601 4.4 47.3 1.0
C7 A:ECN602 4.4 55.9 0.5
N A:ILE450 4.9 52.3 1.0
CD1 A:ILE377 4.9 52.7 1.0
C8 A:ECN602 4.9 58.3 0.5
C10 A:ECN602 5.0 59.0 0.5
N A:GLY451 5.0 52.4 1.0

Iron binding site 2 out of 2 in 3jus

Go back to Iron Binding Sites List in 3jus
Iron binding site 2 out of 2 in the Crystal Structure of Human Lanosterol 14ALPHA-Demethylase (CYP51) in Complex with Econazole


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 Econazole within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe601

b:52.4
occ:1.00
FE B:HEM601 0.0 52.4 1.0
NC B:HEM601 2.0 51.0 1.0
NB B:HEM601 2.0 50.9 1.0
NA B:HEM601 2.1 50.9 1.0
N19 B:ECL600 2.1 66.7 0.5
ND B:HEM601 2.1 51.1 1.0
N19 B:ECN602 2.2 74.9 0.5
SG B:CYS449 2.4 58.3 1.0
C3 B:ECN602 3.0 75.0 0.5
C3 B:ECL600 3.0 66.8 0.5
C1C B:HEM601 3.0 51.3 1.0
C4B B:HEM601 3.0 51.4 1.0
C4C B:HEM601 3.0 50.8 1.0
C1A B:HEM601 3.1 51.5 1.0
C1B B:HEM601 3.1 50.6 1.0
C4D B:HEM601 3.1 51.6 1.0
C4A B:HEM601 3.1 51.1 1.0
C1D B:HEM601 3.1 51.0 1.0
C6 B:ECL600 3.1 66.7 0.5
C6 B:ECN602 3.2 74.9 0.5
CHC B:HEM601 3.4 51.6 1.0
CHA B:HEM601 3.4 52.3 1.0
CHD B:HEM601 3.4 50.8 1.0
CHB B:HEM601 3.5 50.4 1.0
CB B:CYS449 3.5 59.0 1.0
CA B:CYS449 4.1 59.2 1.0
N1 B:ECN602 4.1 75.5 0.5
N1 B:ECL600 4.2 67.4 0.5
C7 B:ECL600 4.2 67.1 0.5
C3C B:HEM601 4.3 51.0 1.0
C2C B:HEM601 4.3 50.8 1.0
C7 B:ECN602 4.3 75.2 0.5
C3B B:HEM601 4.3 51.7 1.0
C2B B:HEM601 4.3 50.6 1.0
C2A B:HEM601 4.3 51.5 1.0
C3A B:HEM601 4.3 51.5 1.0
C2D B:HEM601 4.3 51.0 1.0
C3D B:HEM601 4.3 50.5 1.0
N B:ILE450 4.7 58.9 1.0
CD1 B:ILE377 4.7 57.9 1.0
C8 B:ECN602 4.8 78.1 0.5
N B:GLY451 4.9 58.7 1.0
C B:CYS449 5.0 59.1 1.0

Reference:

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: ESSN 1089-8638
PubMed: 20149798
DOI: 10.1016/J.JMB.2010.01.075
Page generated: Sun Dec 13 15:09:47 2020

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