Crystal structure of LC3 in complex with FAM134B LIR. Determined by X-ray diffraction at 1.8 Å resolution. Released 3 Jun 2015.
Explore 4ZDV in 3D Show helices and sheets RCSB PDB PDBe
4ZDV contains 7 α-helices and 7 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 | 2-4 | 3 | |
| α-helix | 7-10 | 4 | |
| α-helix | 13-26 | 14 | |
| β-strand | 30-37 | 8 | 1 |
| α-helix | 45-47 | 3 | |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 59 | 1 | 2 |
| α-helix | 60-70 | 11 | |
| β-strand | 80-83 | 4 | 1 |
| β-strand | 86-87 | 2 | 1 |
| β-strand | 94 | 1 | 2 |
| α-helix | 95-102 | 8 | |
| α-helix | 108 | 1 | |
| β-strand | 109-114 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Microtubule-associated proteins 1A/1B light chain 3A | A | protein | 132 | Homo sapiens | Q9H492 (AlphaFold model) |
>4ZDV_1 Microtubule-associated proteins 1A/1B light chain 3A (chains A) GPEEGDDFELLDGPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLD KTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGF LYMVYASQETFG
Regulation of endoplasmic reticulum turnover by selective autophagy. Khaminets, A., Heinrich, T., Mari, M. et al. Nature (2015) 522:354-358. DOI 10.1038/nature14498 · PubMed
Other PDB entries of the same protein (UniProt Q9H492 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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