1gdl

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[[Image:1gdl.gif|left|200px]]<br /><applet load="1gdl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gdl.gif|left|200px]]
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caption="1gdl, resolution 1.8&Aring;" />
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'''CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)'''<br />
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{{Structure
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|PDB= 1gdl |SIZE=350|CAPTION= <scene name='initialview01'>1gdl</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NO:NITROGEN OXIDE'>NO</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GDL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GDL OCA].
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1GDL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GDL OCA].
==Reference==
==Reference==
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The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins., Harutyunyan EH, Safonova TN, Kuranova IP, Popov AN, Teplyakov AV, Obmolova GV, Valnshtein BK, Dodson GG, Wilson JC, J Mol Biol. 1996 Nov 22;264(1):152-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8950274 8950274]
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The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins., Harutyunyan EH, Safonova TN, Kuranova IP, Popov AN, Teplyakov AV, Obmolova GV, Valnshtein BK, Dodson GG, Wilson JC, J Mol Biol. 1996 Nov 22;264(1):152-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8950274 8950274]
[[Category: Lupinus luteus]]
[[Category: Lupinus luteus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:45 2008''

Revision as of 09:21, 20 March 2008


PDB ID 1gdl

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)


Overview

Haemoglobins have the ability to discriminate between oxygen and other diatomic molecules. To further understanding of this process the X-ray crystal structures of carbonmonoxy and nitrosyl-leghaemoglobin have been determined at 1.8 A resolution. The ligand geometry is discussed in detail and the controversial issue of bent versus linear carbon monoxide binding is addressed. The bond angle of 160 degrees for CO-leghaemoglobin is in conflict with recent spectroscopy results on myoglobin but is consistent with angles obtained for myoglobin X-ray crystal structures. In contrast to the numerous carbon monoxide studies, very little stereochemical information is available for the nitric oxide adduct of haemoglobin. This is provided by the X-ray structure of NO-leghaemoglobin, which conforms to expected geometry with an Fe-NO angle of 147 degrees and a lengthened iron-proximal histidine bond. Thus crystallographic evidence is given for the predicted weakening of this bond on the binding of nitric oxide.

About this Structure

1GDL is a Single protein structure of sequence from Lupinus luteus. Full crystallographic information is available from OCA.

Reference

The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins., Harutyunyan EH, Safonova TN, Kuranova IP, Popov AN, Teplyakov AV, Obmolova GV, Valnshtein BK, Dodson GG, Wilson JC, J Mol Biol. 1996 Nov 22;264(1):152-61. PMID:8950274

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