1MOL

TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION

Summary for 1MOL

DescriptorMONELLIN (2 entities in total)
Functional Keywordssweet-tasting protein
Biological sourceDioscoreophyllum cumminsii (serendipity berry)
Total number of polymer chains2
Total molecular weight22167.26
Authors
Somoza, J.R.,Kim, S.-H. (deposition date: 1993-04-27, release date: 1994-05-31, Last modification date: 2011-07-13)
Primary citation
Somoza, J.R.,Jiang, F.,Tong, L.,Kang, C.H.,Cho, J.M.,Kim, S.H.
Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution.
J.Mol.Biol., 234:390-404, 1993
PubMed: 8230222 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1993.1594
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.7 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers50.5%4.2%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution