1jnq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jnq.jpg|left|200px]]<br /><applet load="1jnq" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1jnq.jpg|left|200px]]
-
caption="1jnq, resolution 2.1&Aring;" />
+
 
-
'''LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)'''<br />
+
{{Structure
 +
|PDB= 1jnq |SIZE=350|CAPTION= <scene name='initialview01'>1jnq</scene>, resolution 2.1&Aring;
 +
|SITE= <scene name='pdbsite=FE:Fe+(Fe+2)+Active+Site'>FE</scene>
 +
|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=EGT:2-(3,4,5-TRIHYDROXY-PHENYL)-CHROMAN-3,5,7-TRIOL'>EGT</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12]
 +
|GENE=
 +
}}
 +
 
 +
'''LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1JNQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with <scene name='pdbligand=FE2:'>FE2</scene> and <scene name='pdbligand=EGT:'>EGT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] Known structural/functional Site: <scene name='pdbsite=FE:Fe+(Fe+2)+Active+Site'>FE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNQ OCA].
+
1JNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNQ OCA].
==Reference==
==Reference==
-
Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead., Skrzypczak-Jankun E, Zhou K, Jankun J, Int J Mol Med. 2003 Oct;12(4):415-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12964012 12964012]
+
Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead., Skrzypczak-Jankun E, Zhou K, Jankun J, Int J Mol Med. 2003 Oct;12(4):415-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12964012 12964012]
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Lipoxygenase]]
[[Category: Lipoxygenase]]
Line 25: Line 34:
[[Category: purple lipoxygenase]]
[[Category: purple lipoxygenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:40 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:50 2008''

Revision as of 10:05, 20 March 2008


PDB ID 1jnq

Drag the structure with the mouse to rotate
, resolution 2.1Å
Sites:
Ligands: and
Activity: Lipoxygenase, with EC number 1.13.11.12
Coordinates: save as pdb, mmCIF, xml



LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)


Overview

Lipoxygenases (LOXs) are non-heme iron containing enzymes ubiquitous in nature and participating in the metabolism of the polyunsaturated fatty acids (PUFA). They are capable of combining their dioxygenase activity with its co-oxidative activity manifesting itself in biotransformation reactions catalyzed by LOXs for other than PUFA small molecules. LOXs involvement in inflammatory diseases and cancer have been well documented. Catechins are the natural flavonoids of known inhibitory activity toward dioxygenases with a potential to be utilized in disease prevention and treatment. This work presents results obtained from an X-ray analysis of (-)-epigallocatechin gallate (EGCG) interacting with soybean lipoxygenase-3. The 3D structure of the resulting complex reveals the inhibitor depicting (-)-epigallo-catechin that lacks galloyl moiety. The A-ring is near the iron co-factor, attached by the hydrogen bond to the C-terminus of the enzyme, and the B-ring hydroxyl groups participate in the hydrogen bonds and the van der Waals interactions formed by the surrounding amino acids and water molecules.

About this Structure

1JNQ is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead., Skrzypczak-Jankun E, Zhou K, Jankun J, Int J Mol Med. 2003 Oct;12(4):415-20. PMID:12964012

Page seeded by OCA on Thu Mar 20 12:05:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools