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Iron in PDB 3eqm: Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione

Enzymatic activity of Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione

All present enzymatic activity of Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione:
1.14.14.1;

Protein crystallography data

The structure of Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione, PDB code: 3eqm was solved by D.Ghosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.77 / 2.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.208, 140.208, 119.266, 90.00, 90.00, 120.00
R / Rfree (%) 21.4 / 24.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione (pdb code 3eqm). 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 Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione, PDB code: 3eqm:

Iron binding site 1 out of 1 in 3eqm

Go back to Iron Binding Sites List in 3eqm
Iron binding site 1 out of 1 in the Crystal Structure of Human Placental Aromatase Cytochrome P450 in Complex with Androstenedione


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 Placental Aromatase Cytochrome P450 in Complex with Androstenedione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:55.0
occ:1.00
 FE A:HEM600 0.0 55.0 1.0
NC A:HEM600 2.0 52.8 1.0
NB A:HEM600 2.0 53.3 1.0
NA A:HEM600 2.0 52.4 1.0
ND A:HEM600 2.1 53.5 1.0
SG A:CYS437 2.4 63.0 1.0
C4B A:HEM600 3.0 53.9 1.0
C1C A:HEM600 3.0 53.1 1.0
C1A A:HEM600 3.0 52.9 1.0
C4C A:HEM600 3.0 53.5 1.0
C4A A:HEM600 3.1 53.0 1.0
C1B A:HEM600 3.1 52.9 1.0
C1D A:HEM600 3.1 53.8 1.0
C4D A:HEM600 3.1 54.1 1.0
CHC A:HEM600 3.4 53.3 1.0
CB A:CYS437 3.4 62.9 1.0
CHA A:HEM600 3.4 53.4 1.0
CHB A:HEM600 3.4 53.1 1.0
CHD A:HEM600 3.4 53.4 1.0
C19 A:ASD601 4.0 58.9 1.0
CA A:CYS437 4.1 63.0 1.0
C3B A:HEM600 4.2 54.0 1.0
C2C A:HEM600 4.2 53.7 1.0
C3C A:HEM600 4.3 53.9 1.0
C2A A:HEM600 4.3 53.1 1.0
C2B A:HEM600 4.3 53.6 1.0
C3A A:HEM600 4.3 53.1 1.0
C2D A:HEM600 4.3 54.1 1.0
C3D A:HEM600 4.4 54.6 1.0
N A:GLY439 4.7 63.7 1.0
C A:CYS437 4.7 63.2 1.0
N A:ALA438 4.7 63.3 1.0
C1 A:ASD601 4.9 59.9 1.0

Reference:

D.Ghosh, J.Griswold, M.Erman, W.Pangborn. Structural Basis For Androgen Specificity and Oestrogen Synthesis in Human Aromatase. Nature V. 457 219 2009.
ISSN: ISSN 0028-0836
PubMed: 19129847
DOI: 10.1038/NATURE07614
Page generated: Sun Dec 13 15:05:13 2020

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