Crystal structure of the C lobe of E6AP in complex with K48-linked diUb. Determined by X-ray diffraction at 2.59 Å resolution. Released 24 Dec 2025.
Explore 9L3L in 3D Show helices and sheets RCSB PDB PDBe
9L3L contains 14 α-helices and 20 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 767-772 | 6 | |
| β-strand | 775-777 | 3 | 1 |
| α-helix | 785-795 | 11 | |
| α-helix | 799-810 | 12 | |
| α-helix | 815-816 | 2 | |
| α-helix | 820-823 | 4 | |
| β-strand | 826-829 | 4 | 1 |
| α-helix | 836-838 | 3 | |
| β-strand | 839-841 | 3 | 1 |
| β-strand | 846-849 | 4 | 1 |
| α-helix | 855-868 | 14 | |
| β-strand | 869 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 2 |
| β-strand | 12-16 | 5 | 2 |
| β-strand | 22 | 1 | 3 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 2 |
| β-strand | 48-49 | 2 | 2 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 3 |
| β-strand | 66-71 | 6 | 2 |
| β-strand | 74 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 4 |
| β-strand | 12-16 | 5 | 4 |
| β-strand | 22 | 1 | 5 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 4 |
| β-strand | 48-49 | 2 | 4 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 5 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-protein ligase E3A | A | protein | 108 | Homo sapiens | Q05086 (AlphaFold model) |
| Donor Ubiquitin | B | protein | 76 | Homo sapiens | P62979 (AlphaFold model) |
| Acceptor Ubiquitin | C | protein | 73 | Homo sapiens | P62979 (AlphaFold model) |
>9L3L_1 Ubiquitin-protein ligase E3A (chains A) LDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLK MIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGF
>9L3L_2 Donor Ubiquitin (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>9L3L_3 Acceptor Ubiquitin (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRL
Structural Insights into the Role of the C-Lobe of E6AP in Catalyzing K48-Linked Ubiquitin Chain Formation. Wu, X.W., Cai, H.Y., Du, Y.X. et al. To be published.
Other PDB entries of the same protein (UniProt Q05086 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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