9R6V
Crystal structure of the DOC domain of the E3 ligase HECTD3
Summary for 9R6V
| Entry DOI | 10.2210/pdb9r6v/pdb |
| Descriptor | E3 ubiquitin-protein ligase HECTD3, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | e3-ligase, ubiquitin, ubiquitination, hect-ligase, ligase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 32174.94 |
| Authors | Esposito, D.,Huber, J.,Maslen, S.,Rittinger, K. (deposition date: 2025-05-13, release date: 2026-01-28, Last modification date: 2026-03-04) |
| Primary citation | Huber, J.,Esposito, D.,Maslen, S.,Chambers, D.O.,Skehel, J.M.,Rittinger, K. Structure and mechanism of the HECT ligase HECTD3. Nat Commun, 2026 Cited by PubMed Abstract: HECT E3 ligases regulate many cellular processes, yet how they recognise their substrates and synthesise specific types of poly-ubiquitin chains is still incompletely understood. HECTD3, a member of the "other HECT" family, is implicated in the regulation of inflammation, apoptosis, and infection and highly expressed in several cancers. These functions are largely attributed to its ligase activity and modification of diverse substrates with different types of ubiquitin chains. We present a detailed analysis of the ligase activity of HECTD3, including its ubiquitin linkage preferences, oligomeric state and substrate ubiquitination. Using cryo-EM, we provide the full-length structures of HECTD3 in both apo and ubiquitin-loaded forms, revealing key insights into its domain organisation, including discovery of a distinct fold of the N-terminal region, and mechanistic features. Some of these are shared with other HECT ligases, while others are unique to HECTD3 and contribute to differences in its catalytic mechanisms and functional diversity. PubMed: 41690955DOI: 10.1038/s41467-026-69520-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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