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Atomistry » Iron » PDB 2r1m-2rfb » 2rcm » |
Iron in PDB 2rcm: Crystal Structure of Arabidopsis Thaliana Allene Oxide Synthase Variant (F137L) (at-Aos(F137L), Cytochrome P450 74A) at 1.73 A ResolutionEnzymatic 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:
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 2rcmGo 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
Iron binding site 2 out of 2 in 2rcmGo 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
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.
Page generated: Sun Dec 13 14:52:40 2020
ISSN: ISSN 0028-0836 PubMed: 18716621 DOI: 10.1038/NATURE07307 |
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