The cryo-EM structure of the ERAD retrotranslocation channel formed by human Derlin-1. Determined by electron microscopy at 3.8 Å resolution. Released 17 Mar 2021.
Explore 7CZB in 3D Show helices and sheets RCSB PDB PDBe
7CZB contains 40 α-helices and 6 β-strands across 4 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 | 17-31 | 15 | |
| α-helix | 36-38 | 3 | |
| α-helix | 43-48 | 6 | |
| α-helix | 58-60 | 3 | |
| α-helix | 70-88 | 19 | |
| α-helix | 95-104 | 10 | |
| α-helix | 106-115 | 10 | |
| α-helix | 123-135 | 13 | |
| α-helix | 150-151 | 2 | |
| α-helix | 155-165 | 11 | |
| α-helix | 171-187 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-30 | 14 | |
| α-helix | 36-38 | 3 | |
| α-helix | 44-47 | 4 | |
| α-helix | 54-57 | 4 | |
| β-strand | 65 | 1 | 1 |
| β-strand | 68 | 1 | 1 |
| α-helix | 71-89 | 19 | |
| α-helix | 95-115 | 21 | |
| α-helix | 123-136 | 14 | |
| β-strand | 142 | 1 | 2 |
| β-strand | 149 | 1 | 2 |
| α-helix | 155-166 | 12 | |
| α-helix | 174-188 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-30 | 14 | |
| α-helix | 36-38 | 3 | |
| α-helix | 44-47 | 4 | |
| α-helix | 54-57 | 4 | |
| β-strand | 65 | 1 | 3 |
| β-strand | 68 | 1 | 3 |
| α-helix | 71-89 | 19 | |
| α-helix | 95-115 | 21 | |
| α-helix | 123-136 | 14 | |
| α-helix | 155-166 | 12 | |
| α-helix | 174-188 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Derlin-1 | A, B, C, D | protein | 251 | Homo sapiens | Q9BUN8 (AlphaFold model) |
>7CZB_1 Derlin-1 (chains A, B, C, D) MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATF YFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQL LMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVG HLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRH NWGQGFRLGDQ
The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1. Rao, B., Li, S., Yao, D. et al. Sci Adv (2021) 7. DOI 10.1126/sciadv.abe8591 · PubMed
Other PDB entries of the same protein (UniProt Q9BUN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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