1p5j

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Image:1p5j.gif

1p5j, resolution 2.5Å

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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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