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3TDZ

N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-stapled acetylated Ubc12N complex

Summary for 3TDZ
Entry DOI10.2210/pdb3tdz/pdb
Related3TDI 3TDU
Related PRD IDPRD_001077
DescriptorDCN1-like protein 1, Cullin-1, STAPLED PEPTIDE, ... (4 entities in total)
Functional Keywordse2:e3, protein binding-inhibitor complex, protein binding/inhibitor
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus : Q96GG9
Total number of polymer chains6
Total formula weight67602.14
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: 2023-12-06)
Primary citationScott, 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 (2 Å)
Structure validation

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