Crystal structure of human AMSH-LP DUB domain in complex with Lys63-linked ubiquitin dimer

Summary for 2ZNV

DescriptorAMSH-like protease, Ubiquitin, ZINC ION, ... (6 entities in total)
Functional Keywordsprotein complex, metal binding protein, alternative splicing, hydrolase, metal-binding, metalloprotease, protease, ubl conjugation pathway, zinc, cytoplasm, nucleus, phosphoprotein, hydrolase-signaling protein complex, hydrolase/signaling protein
Biological sourceHomo sapiens (human)
Total number of polymer chains6
Total molecular weight74743.01
Sato, Y.,Azusa, Y.,Yamagata, A.,Mimura, H.,Wang, X.,Yamashita, M.,Ookata, K.,Nureki, O.,Iwai, K.,Komada, M.,Fukai, S. (deposition date: 2008-05-01, release date: 2008-09-02, Last modification date: 2011-07-13)
Primary citation
Sato, Y.,Yoshikawa, A.,Yamagata, A.,Mimura, H.,Yamashita, M.,Ookata, K.,Nureki, O.,Iwai, K.,Komada, M.,Fukai, S.
Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
Nature, 455:358-362, 2008
PubMed: 18758443 (PDB entries with the same primary citation)
DOI: 10.1038/nature07254
MImport into Mendeley
Experimental method
NMR Information

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.21540.2%1.9%4.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report