NMR structure of the RING domain in ubiquitin ligase gp78. Determined by solution NMR. Released 28 Aug 2013.
Explore 2LXH in 3D Show helices and sheets RCSB PDB PDBe
2LXH contains 2 α-helices and 4 β-strands across 1 chain. 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 | 332-337 | 6 | |
| β-strand | 352-353 | 2 | 1 |
| β-strand | 359-360 | 2 | 1 |
| α-helix | 362-371 | 10 | |
| β-strand | 374 | 1 | 2 |
| β-strand | 381 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase AMFR | C | protein | 81 | Homo sapiens | Q9UKV5 (AlphaFold model) |
>2LXH_1 E3 ubiquitin-protein ligase AMFR (chains C) KNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQD TSCPTCRMSLNIADNNRVREE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. Das, R., Liang, Y.H., Mariano, J. et al. EMBO J (2013) 32:2504-2516. DOI 10.1038/emboj.2013.174 · PubMed
Other PDB entries of the same protein (UniProt Q9UKV5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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