1ed6

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[[Image:1ed6.gif|left|200px]]<br /><applet load="1ed6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ed6.gif|left|200px]]
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caption="1ed6, resolution 2.05&Aring;" />
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'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)'''<br />
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{{Structure
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|PDB= 1ed6 |SIZE=350|CAPTION= <scene name='initialview01'>1ed6</scene>, resolution 2.05&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ILO:N5-IMINOETHYL-L-ORNITHINE'>ILO</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39]
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|GENE=
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}}
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'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ED6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=ILO:'>ILO</scene>, <scene name='pdbligand=CAD:'>CAD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED6 OCA].
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1ED6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11331003 11331003]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11331003 11331003]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
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[[Category: nitric oxide synthase]]
[[Category: nitric oxide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:57 2008''

Revision as of 08:53, 20 March 2008


PDB ID 1ed6

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands: , , , , and
Activity: Nitric-oxide synthase, with EC number 1.14.13.39
Coordinates: save as pdb, mmCIF, xml



BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (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.

About this Structure

1ED6 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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

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