Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Determined by solution NMR. Released 26 Jul 2005.
Explore 1ZC1 in 3D Show helices and sheets RCSB PDB PDBe
1ZC1 contains 10 α-helices and 15 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 | 16-18 | 3 | |
| β-strand | 19-29 | 11 | 1 |
| α-helix | 30-32 | 3 | |
| α-helix | 40-44 | 5 | |
| β-strand | 47-48 | 2 | 2 |
| β-strand | 49 | 1 | 1 |
| β-strand | 50 | 1 | 2 |
| α-helix | 52-60 | 9 | |
| α-helix | 63-64 | 2 | |
| α-helix | 67 | 1 | |
| β-strand | 69-72 | 4 | 1 |
| β-strand | 79-82 | 4 | 1 |
| β-strand | 83-87 | 5 | 2 |
| β-strand | 93-96 | 4 | 1 |
| α-helix | 98-104 | 7 | |
| β-strand | 111-118 | 8 | 1 |
| β-strand | 124-128 | 5 | 3 |
| α-helix | 131-135 | 5 | |
| α-helix | 140-150 | 11 | |
| β-strand | 154-155 | 2 | 4 |
| β-strand | 159-164 | 6 | 3 |
| β-strand | 167-177 | 11 | 3 |
| β-strand | 184-185 | 2 | 4 |
| β-strand | 193-196 | 4 | 3 |
| α-helix | 204-207 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin fusion degradation protein 1 | A | protein | 208 | Saccharomyces cerevisiae | P53044 (AlphaFold model) |
>1ZC1_1 Ubiquitin fusion degradation protein 1 (chains A) MFSGFSSFGGGNGFVNMPQTFEEFFRCYPIAMMNDRIRKDDANFGGKIFLPPSALSKLSM LNIRYPMLFKLTANETGRVTHGGVLEFIAEEGRVYLPQWMMETLGIQPGSLLQISSTDVP LGQFVKLEPQSVDFLDISDPKAVLENVLRNFSTLTVDDVIEISYNGKTFKIKILEVKPES SSKSICVIETDLVTDFAPPVGYVEPDYK
Ufd1 Exhibits the AAA-ATPase Fold with Two Distinct Ubiquitin Interaction Sites. Park, S., Isaacson, R., Kim, H.T. et al. Structure (2005) 13:995-1005. DOI 10.1016/j.str.2005.04.013 · PubMed
Other PDB entries of the same protein (UniProt P53044 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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