3TDU
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex
Summary for 3TDU
Entry DOI | 10.2210/pdb3tdu/pdb |
Related | 3TDI 3TDZ |
Descriptor | DCN1-like protein 1, Cullin-1, NEDD8-conjugating enzyme Ubc12, ... (4 entities in total) |
Functional Keywords | e2:e3, ligase-protein binding complex, ligase/protein binding |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 6 |
Total formula weight | 68324.90 |
Authors | Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A. (deposition date: 2011-08-11, release date: 2011-10-12, Last modification date: 2024-03-13) |
Primary citation | Scott, D.C.,Monda, J.K.,Bennett, E.J.,Harper, J.W.,Schulman, B.A. N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science, 334:674-678, 2011 Cited by PubMed: 21940857DOI: 10.1126/science.1209307 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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