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5GOG

Lys29-linked di-ubiquitin

Summary for 5GOG
Entry DOI10.2210/pdb5gog/pdb
Related5GO7 5GO8 5GOB 5GOC 5GOD 5GOH 5GOI 5GOJ 5GOK
DescriptorUbiquitin, D-ubiquitin (3 entities in total)
Functional Keywordspolyubiquitin chains, quasi-racemic crystal, protein binding
Biological sourceHomo sapiens (Human)
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Cellular locationUbiquitin: Cytoplasm : P0CG47
Total number of polymer chains2
Total formula weight17128.58
Authors
Gao, S.,Pan, M.,Zheng, Y. (deposition date: 2016-07-27, release date: 2016-11-02, Last modification date: 2023-11-15)
Primary citationGao, S.,Pan, M.,Zheng, Y.,Huang, Y.,Zheng, Q.,Sun, D.,Lu, L.,Tan, X.,Tan, X.,Lan, H.,Wang, J.,Wang, T.,Wang, J.,Liu, L.
Monomer/Oligomer Quasi-Racemic Protein Crystallography
J.Am.Chem.Soc., 138:14497-14502, 2016
Cited by
PubMed Abstract: Racemic or quasi-racemic crystallography recently emerges as a useful technology for solution of the crystal structures of biomacromolecules. It remains unclear to what extent the biomacromolecules of opposite handedness can differ from each other in racemic or quasi-racemic crystallography. Here we report a finding that monomeric d-ubiquitin (Ub) has propensity to cocrystallize with different dimers, trimers, and even a tetramer of l-Ub. In these cocrystals the unconnected monomeric d-Ubs can self-assemble to form pseudomirror images of different oligomers of l-Ub. This monomer/oligomer cocrystallization phenomenon expands the concept of racemic crystallography. Using the monomer/oligomer cocrystallization technology we obtained, for the first time the X-ray structures of linear M1-linked tri- and tetra-Ubs and a K11/K63-branched tri-Ub.
PubMed: 27768314
DOI: 10.1021/jacs.6b09545
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.977 Å)
Structure validation

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