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3FO5

Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)

Summary for 3FO5
Entry DOI10.2210/pdb3fo5/pdb
DescriptorThioesterase, adipose associated, isoform BFIT2, PENTAETHYLENE GLYCOL, CHLORIDE ION, ... (6 entities in total)
Functional Keywordsorthogonal bundle, consortium, lipid transport
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight60191.24
Authors
Primary citationThorsell, A.G.,Lee, W.H.,Persson, C.,Siponen, M.I.,Nilsson, M.,Busam, R.D.,Kotenyova, T.,Schuler, H.,Lehtio, L.
Comparative structural analysis of lipid binding START domains.
Plos One, 6:e19521-e19521, 2011
Cited by
PubMed Abstract: Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease.
PubMed: 21738568
DOI: 10.1371/journal.pone.0019521
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

数据于2024-10-30公开中

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