1bgi

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[[Image:1bgi.gif|left|200px]]<br /><applet load="1bgi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bgi.gif|left|200px]]
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caption="1bgi, resolution 1.7&Aring;" />
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'''ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)'''<br />
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{{Structure
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|PDB= 1bgi |SIZE=350|CAPTION= <scene name='initialview01'>1bgi</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
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|GENE=
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}}
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'''ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGI OCA].
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1BGI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGI OCA].
==Reference==
==Reference==
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Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10089401 10089401]
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Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089401 10089401]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: o-glycosyl]]
[[Category: o-glycosyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:40 2008''

Revision as of 08:10, 20 March 2008


PDB ID 1bgi

Drag the structure with the mouse to rotate
, resolution 1.7Å
Ligands:
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)


Overview

The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.

About this Structure

1BGI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401

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