The crystal structure of the DUB domain of AMSH orthologue, Sst2 from S. pombe, in complex with lysine 63-linked diubiquitin

Summary for 4NQL

Related2ZNV 3RZV 4MSQ 4MSM
DescriptorAMSH-like protease sst2, Ubiquitin, ZINC ION, ... (6 entities in total)
Functional Keywordsjamm domain, zinc metalloprotease, protein complex, amsh, heix-beta-helix sandwich, hydrolase, metal binding, k63-linked diubiquitin, helix-beta-helix sandwich, deubiquitinase, ubiquitin, hse1, cytosol, endosome, hydrolase-protein binding complex, hydrolase/protein binding
Biological sourceSchizosaccharomyces pombe (Fission yeast)
Cellular locationCytoplasm Q9P371
Cytoplasm (By similarity) P0CG50 P0CG50
Total number of polymer chains3
Total molecular weight42457.62
Ronau, J.A.,Shrestha, R.K.,Das, C. (deposition date: 2013-11-25, release date: 2014-10-08)
Primary citation
Shrestha, R.K.,Ronau, J.A.,Davies, C.W.,Guenette, R.G.,Strieter, E.R.,Paul, L.N.,Das, C.
Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product.
Biochemistry, 53:3199-3217, 2014
PubMed: 24787148 (PDB entries with the same primary citation)
DOI: 10.1021/bi5003162
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.261101.9%6.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report