Iron in PDB 3cli: Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution

All present enzymatic activity of Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution:
4.2.1.92;

The structure of Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution, PDB code: 3cli 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 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.639, 105.192, 162.295, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.8

The binding sites of Iron atom in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution (pdb code 3cli). 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 (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution, PDB code: 3cli:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 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 (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe600 b:15.6 occ:1.00 FE A:HEM600 0.0 15.6 1.0 NA A:HEM600 2.1 15.5 1.0 NC A:HEM600 2.1 16.1 1.0 ND A:HEM600 2.1 13.8 1.0 NB A:HEM600 2.1 14.9 1.0 SG A:CYS471 2.4 18.8 1.0 C1D A:HEM600 3.1 15.7 1.0 C4C A:HEM600 3.1 14.7 1.0 C1C A:HEM600 3.1 15.2 1.0 C1B A:HEM600 3.1 17.2 1.0 C4B A:HEM600 3.1 15.7 1.0 C4A A:HEM600 3.1 15.7 1.0 C4D A:HEM600 3.1 14.7 1.0 C1A A:HEM600 3.1 15.7 1.0 CB A:CYS471 3.4 17.5 1.0 CHD A:HEM600 3.4 15.3 1.0 CHB A:HEM600 3.4 15.2 1.0 CHC A:HEM600 3.4 14.8 1.0 CHA A:HEM600 3.5 14.4 1.0 O A:HOH860 3.6 23.6 1.0 CA A:CYS471 4.0 17.3 1.0 C2C A:HEM600 4.3 16.4 1.0 C3C A:HEM600 4.3 16.1 1.0 C2D A:HEM600 4.3 16.0 1.0 C2B A:HEM600 4.3 16.2 1.0 C3A A:HEM600 4.3 15.3 1.0 CB A:ASN321 4.3 19.4 1.0 C3B A:HEM600 4.3 16.8 1.0 C3D A:HEM600 4.3 14.0 1.0 C2A A:HEM600 4.4 14.3 1.0 ND2 A:ASN321 4.4 22.1 1.0 N A:ALA472 4.6 17.2 1.0 C A:CYS471 4.6 17.3 1.0 CG A:ASN321 4.7 21.8 1.0 N A:GLY473 4.8 19.1 1.0 O A:HOH859 4.8 22.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase (Aos, Cytochrome P450 74A, CYP74A) at 1.80 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 (Aos, Cytochrome P450 74A, CYP74A) at 1.80 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:15.6 occ:1.00 FE B:HEM600 0.0 15.6 1.0 NC B:HEM600 2.1 16.3 1.0 NA B:HEM600 2.1 15.8 1.0 ND B:HEM600 2.1 14.4 1.0 NB B:HEM600 2.1 13.6 1.0 SG B:CYS471 2.3 18.8 1.0 C1C B:HEM600 3.0 15.3 1.0 C4C B:HEM600 3.1 15.6 1.0 C1D B:HEM600 3.1 15.2 1.0 C1B B:HEM600 3.1 14.6 1.0 C4B B:HEM600 3.1 13.9 1.0 C4D B:HEM600 3.1 14.3 1.0 C1A B:HEM600 3.1 14.8 1.0 C4A B:HEM600 3.2 15.1 1.0 CB B:CYS471 3.3 18.2 1.0 CHC B:HEM600 3.4 14.9 1.0 CHD B:HEM600 3.4 13.7 1.0 CHA B:HEM600 3.5 14.0 1.0 CHB B:HEM600 3.5 14.7 1.0 O B:HOH1237 3.9 22.4 1.0 CA B:CYS471 3.9 17.9 1.0 C2C B:HEM600 4.2 15.9 1.0 C3C B:HEM600 4.3 15.4 1.0 CB B:ASN321 4.3 20.5 1.0 C2D B:HEM600 4.3 15.0 1.0 C2B B:HEM600 4.3 13.1 1.0 C3D B:HEM600 4.3 15.6 1.0 C3B B:HEM600 4.3 14.0 1.0 C2A B:HEM600 4.4 14.9 1.0 C3A B:HEM600 4.4 14.3 1.0 ND2 B:ASN321 4.4 24.9 1.0 N B:ALA472 4.5 18.2 1.0 C B:CYS471 4.6 18.2 1.0 CG B:ASN321 4.7 23.1 1.0 N B:GLY473 4.8 19.6 1.0 O B:HOH1236 5.0 19.0 1.0

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