3BQP

Crystal Structure of Human Saposin D (orthorhombic)

Summary for 3BQP

Entry DOI	10.2210/pdb3bqp/pdb
Related	3BQQ
Descriptor	Proactivator polypeptide, MAGNESIUM ION (3 entities in total)
Functional Keywords	saposin, sphingolipid activator protein, lipid binding protein, acid ceramidase, farber disease, lipid metabolism, lysosome, sphingolipid metabolism
Biological source	Homo sapiens (human)
Cellular location	Lysosome: P07602
Total number of polymer chains	2
Total formula weight	17925.58
Authors	Prive, G.G.,Popovic, K. (deposition date: 2007-12-20, release date: 2008-02-05, Last modification date: 2024-10-30)
Primary citation	Popovic, K.,Prive, G.G. Structures of the human ceramide activator protein saposin D. Acta Crystallogr.,Sect.D, 64:589-594, 2008 Cited by PubMed Abstract: Saposin D is a sphingolipid activator protein required for the lysosomal breakdown of ceramide to a fatty acid and sphingosine by acid ceramidase. The crystal structure of saposin D has been determined in two different crystal forms, resulting in a total of six crystallographically independent views of this small 80-amino-acid protein. All of the structures are highly similar and reveal the monomeric form of the saposin fold previously seen in the crystal structures of saposins A and C. Saposin D is slightly more compact than the related saposins A and C owing to a slight repositioning of the 'stem' and 'hairpin' regions of the protein. PubMed: 18453694 DOI: 10.1107/S0907444908003120 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.3 Å)

Structure validation