1fol: Difference between revisions

Revision as of 03:41, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fol.png

Template:STRUCTURE 1fol

REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)

Template:ABSTRACT PUBMED 11331003

About this StructureAbout this Structure

1FOL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003

Page seeded by OCA on Tue Jul 1 03:41:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fol.gif|left|200px]]
+{{Seed}}
+[[Image:1fol.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fol|  PDB=1fol  |  SCENE=  }}
-'''REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)'''
+===REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)===
-==Overview==
+<!--
-The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
+The line below this paragraph, {{ABSTRACT_PUBMED_11331003}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11331003 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11331003}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Alpha-beta fold]]
 [[Category: Nitric oxide synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:34:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:41:35 2008''