1P5J

Crystal Structure Analysis of Human Serine Dehydratase

Summary for 1P5J

• Entry DOI: 10.2210/pdb1p5j/pdb
• Descriptor: L-serine dehydratase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: lyase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 39805.80

Authors

Sun, L.,Liu, Y.,Rao, Z. (deposition date: 2003-04-27, release date: 2004-06-01, Last modification date: 2023-10-25)

Primary citation

Sun, L.,Li, X.,Dong, Y.,Yang, M.,Liu, Y.,Han, X.,Zhang, X.,Pang, H.,Rao, Z.
Crystallization and preliminary crystallographic analysis of human serine dehydratase.
Acta Crystallogr.,Sect.D, 59:2297-2299, 2003

PubMed Abstract: 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%.

PubMed: 14646100
DOI: 10.1107/S0907444903020110

Experimental method

X-RAY DIFFRACTION (2.5 Å)