4LDT

The structure of h/ceOTUB1-ubiquitin aldehyde-UBCH5B~Ub

Summary for 4LDT

DescriptorUbiquitin thioesterase otubain-like, Ubiquitin aldehyde, Ubiquitin-conjugating enzyme E2 D2, ... (7 entities in total)
Functional Keywordsisopeptidase, ubiquitin-conjugating, post-translational modification, ubiquitin, ubiquitin-aldehyde, hydrolase regulator
Biological sourceHomo sapiens (human, nematode)
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Cellular locationUbiquitin: Cytoplasm  P0CG48 P0CG48
Total number of polymer chains4
Total molecular weight67002.09
Authors
Wiener, R.,DiBello, A.T.,Lombardi, P.M.,Guzzo, C.M.,Zhang, X.,Matunis, M.J.,Wolberger, C. (deposition date: 2013-06-25, release date: 2013-08-14, Last modification date: 2017-07-26)
Primary citation
Wiener, R.,Dibello, A.T.,Lombardi, P.M.,Guzzo, C.M.,Zhang, X.,Matunis, M.J.,Wolberger, C.
E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1.
Nat.Struct.Mol.Biol., 20:1033-1039, 2013
PubMed: 23955022 (PDB entries with the same primary citation)
DOI: 10.1038/nsmb.2655
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.901 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.227200.9%6.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report