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: 21940857 DOI: 10.1126/science.1209307 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation