Crystal structure of the S18Y variant of ubiquitin carboxy terminal hydrolase L1 bound to ubiquitin vinylmethylester.

Summary for 3IFW

DescriptorUbiquitin carboxyl-terminal hydrolase isozyme L1, Ubiquitin, METHYL 4-AMINOBUTANOATE, ... (4 entities in total)
Functional Keywordsenzyme-suicide substrate complex, cytoplasm, disease mutation, glycoprotein, hydrolase, ligase, oxidation, polymorphism, protease, thiol protease, ubl conjugation pathway, isopeptide bond, nucleus, phosphoprotein, ubl conjugation, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm P09936
Total number of polymer chains2
Total molecular weight33979.82
Das, C.,Boudreaux, D.,Maiti, T. (deposition date: 2009-07-26, release date: 2010-06-16, Last modification date: 2011-07-13)
Primary citation
Boudreaux, D.A.,Maiti, T.K.,Davies, C.W.,Das, C.
Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation.
Proc.Natl.Acad.Sci.USA, 107:9117-9122, 2010
PubMed: 20439756 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.0910870107
MImport into Mendeley
Experimental method
NMR Information

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.25630.3%3.5%2.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report