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Iron in PDB 2rcm: Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution

Enzymatic activity of Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution:
4.2.1.92;

Protein crystallography data

The structure of Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution, PDB code: 2rcm was solved by D.S.Lee, P.Nioche, C.S.Raman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.39 / 1.73
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.454, 105.275, 162.485, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution (pdb code 2rcm). 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 Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution, PDB code: 2rcm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2rcm

Go back to Iron Binding Sites List in 2rcm
Iron binding site 1 out of 2 in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution


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 Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:15.8
occ:1.00
 FE A:HEM600 0.0 15.8 1.0
NA A:HEM600 2.1 16.3 1.0
NC A:HEM600 2.1 16.6 1.0
ND A:HEM600 2.1 14.2 1.0
NB A:HEM600 2.1 14.9 1.0
SG A:CYS471 2.4 20.6 1.0
C4B A:HEM600 3.0 14.7 1.0
C1C A:HEM600 3.1 14.6 1.0
C1D A:HEM600 3.1 16.6 1.0
C4D A:HEM600 3.1 14.9 1.0
C4C A:HEM600 3.1 15.9 1.0
C1A A:HEM600 3.1 16.0 1.0
C4A A:HEM600 3.1 15.8 1.0
C1B A:HEM600 3.1 15.7 1.0
CB A:CYS471 3.4 19.7 1.0
CHC A:HEM600 3.4 16.1 1.0
CHA A:HEM600 3.4 17.1 1.0
CHD A:HEM600 3.4 16.9 1.0
CHB A:HEM600 3.5 17.3 1.0
O A:HOH953 3.9 25.8 1.0
CA A:CYS471 4.0 19.8 1.0
C2C A:HEM600 4.2 16.9 1.0
C3C A:HEM600 4.3 16.7 1.0
C3B A:HEM600 4.3 15.8 1.0
CB A:ASN321 4.3 21.4 1.0
C2D A:HEM600 4.3 16.4 1.0
C2B A:HEM600 4.3 16.5 1.0
C3D A:HEM600 4.3 15.2 1.0
C3A A:HEM600 4.3 16.4 1.0
C2A A:HEM600 4.3 15.5 1.0
ND2 A:ASN321 4.5 25.9 1.0
N A:ALA472 4.6 20.4 1.0
C A:CYS471 4.6 19.7 1.0
CG A:ASN321 4.7 23.8 1.0
N A:GLY473 4.8 20.6 1.0
O A:HOH952 4.9 24.0 1.0

Iron binding site 2 out of 2 in 2rcm

Go back to Iron Binding Sites List in 2rcm
Iron binding site 2 out of 2 in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution


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 Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:16.1
occ:1.00
 FE B:HEM600 0.0 16.1 1.0
NB B:HEM600 2.1 14.8 1.0
NA B:HEM600 2.1 15.9 1.0
NC B:HEM600 2.1 16.2 1.0
ND B:HEM600 2.1 14.7 1.0
SG B:CYS471 2.4 21.1 1.0
C1C B:HEM600 3.0 14.8 1.0
C1D B:HEM600 3.1 15.8 1.0
C4B B:HEM600 3.1 16.5 1.0
C1B B:HEM600 3.1 17.0 1.0
C4C B:HEM600 3.1 16.8 1.0
C4A B:HEM600 3.1 16.6 1.0
C4D B:HEM600 3.1 15.9 1.0
C1A B:HEM600 3.1 15.9 1.0
CB B:CYS471 3.3 21.4 1.0
CHC B:HEM600 3.4 14.7 1.0
CHD B:HEM600 3.4 15.5 1.0
CHB B:HEM600 3.4 16.7 1.0
CHA B:HEM600 3.5 14.6 1.0
CA B:CYS471 3.9 20.4 1.0
O B:HOH838 4.1 25.4 1.0
CB B:ASN321 4.2 21.9 1.0
C2C B:HEM600 4.2 15.8 1.0
C3C B:HEM600 4.3 17.8 1.0
C2B B:HEM600 4.3 15.0 1.0
C3B B:HEM600 4.3 16.1 1.0
C2D B:HEM600 4.3 16.2 1.0
C3D B:HEM600 4.3 16.8 1.0
C3A B:HEM600 4.3 16.9 1.0
C2A B:HEM600 4.4 16.1 1.0
ND2 B:ASN321 4.5 25.4 1.0
N B:ALA472 4.5 20.4 1.0
C B:CYS471 4.6 20.9 1.0
CG B:ASN321 4.6 24.5 1.0
N B:GLY473 4.8 21.4 1.0

Reference:

D.S.Lee, P.Nioche, M.Hamberg, C.S.Raman. Structural Insights Into the Evolutionary Paths of Oxylipin Biosynthetic Enzymes. Nature V. 455 363 2008.
ISSN: ISSN 0028-0836
PubMed: 18716621
DOI: 10.1038/NATURE07307
Page generated: Sun Aug 4 02:09:14 2024

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