1p5j

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(New page: 200px<br /> <applet load="1p5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5j, resolution 2.5&Aring;" /> '''Crystal Structure An...)
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<applet load="1p5j" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1p5j, resolution 2.5&Aring;" />
caption="1p5j, resolution 2.5&Aring;" />
'''Crystal Structure Analysis of Human Serine Dehydratase'''<br />
'''Crystal Structure Analysis of Human Serine Dehydratase'''<br />
==Overview==
==Overview==
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L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP), dependent deamination of L-serine to yield pyruvate. Recombinant human, serine dehydratase was crystallized by the hanging-drop vapour-diffusion, method. Crystals were grown at 291 K using (NH4)(2)SO4 as precipitant., Diffraction data were obtained to a resolution of 2.5 A from a single, frozen crystal using Cu Kalpha radiation. The crystal belongs to space, group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains one, molecule and has a solvent content of about 46%.
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L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP) dependent deamination of L-serine to yield pyruvate. Recombinant human serine dehydratase was crystallized by the hanging-drop vapour-diffusion method. Crystals were grown at 291 K using (NH4)(2)SO4 as precipitant. Diffraction data were obtained to a resolution of 2.5 A from a single frozen crystal using Cu Kalpha radiation. The crystal belongs to space group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains one molecule and has a solvent content of about 46%.
==Disease==
==Disease==
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Known diseases associated with this structure: Paraganglioma, familial chromaffin, 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185470 185470]], Pheochromocytoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185470 185470]], Shwachman-Bodian-Diamond syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607444 607444]]
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Known diseases associated with this structure: Paraganglioma and gastric stromal sarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185470 185470]], Paraganglioma, familial chromaffin, 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185470 185470]], Pheochromocytoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185470 185470]], Shwachman-Bodian-Diamond syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607444 607444]]
==About this Structure==
==About this Structure==
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1P5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/L-serine_ammonia-lyase L-serine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.17 4.3.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P5J OCA].
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1P5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/L-serine_ammonia-lyase L-serine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.17 4.3.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5J OCA].
==Reference==
==Reference==
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[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:40:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:18 2008''

Revision as of 12:25, 21 February 2008

Image:1p5j.gif

1p5j, resolution 2.5Å

Drag the structure with the mouse to rotate

Crystal Structure Analysis of Human Serine Dehydratase

Contents

Overview

L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP) dependent deamination of L-serine to yield pyruvate. Recombinant human serine dehydratase was crystallized by the hanging-drop vapour-diffusion method. Crystals were grown at 291 K using (NH4)(2)SO4 as precipitant. Diffraction data were obtained to a resolution of 2.5 A from a single frozen crystal using Cu Kalpha radiation. The crystal belongs to space group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains one molecule and has a solvent content of about 46%.

Disease

Known diseases associated with this structure: Paraganglioma and gastric stromal sarcoma OMIM:[185470], Paraganglioma, familial chromaffin, 4 OMIM:[185470], Pheochromocytoma OMIM:[185470], Shwachman-Bodian-Diamond syndrome OMIM:[607444]

About this Structure

1P5J is a Single protein structure of sequence from Homo sapiens with as ligand. Active as L-serine ammonia-lyase, with EC number 4.3.1.17 Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary crystallographic analysis of human serine dehydratase., Sun L, Li X, Dong Y, Yang M, Liu Y, Han X, Zhang X, Pang H, Rao Z, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. Epub 2003, Nov 27. PMID:14646100

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