Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding

Summary for 4FMM

DescriptorPhosphatidylinositol transfer protein PDR16, GLYCEROL, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordssec14 domain, phosphatidylinositol binding, signaling protein, lipid binding protein
Biological sourceSaccharomyces cerevisiae (yeast)
Cellular locationLipid droplet P53860
Total number of polymer chains2
Total molecular weight84878.22
Yuan, Y.,Zhao, W.,Wang, X.,Gao, Y.,Niu, L.,Teng, M. (deposition date: 2012-06-18, release date: 2013-02-27, Last modification date: 2013-06-19)
Primary citation
Yuan, Y.,Zhao, W.,Wang, X.,Gao, Y.,Niu, L.,Teng, M.
Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding.
Acta Crystallogr.,Sect.D, 69:313-323, 2013
PubMed: 23519406 (PDB entries with the same primary citation)
DOI: 10.1107/S0907444912046161
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.255704.6%0.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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