X-ray structure of the RNase domain of the yeast Pop2 protein. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Nov 2003.
Explore 1UOC in 3D Show helices and sheets RCSB PDB PDBe
1UOC contains 32 α-helices and 20 β-strands across 2 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 | 11-14 | 4 | |
| β-strand | 17-19 | 3 | 1 |
| α-helix | 24-34 | 11 | |
| β-strand | 40-48 | 9 | 1 |
| α-helix | 61-73 | 13 | |
| β-strand | 77-86 | 10 | 1 |
| β-strand | 99-103 | 5 | 1 |
| β-strand | 104 | 1 | 2 |
| α-helix | 115-123 | 9 | |
| α-helix | 128-134 | 7 | |
| α-helix | 135 | 1 | |
| β-strand | 136 | 1 | 2 |
| α-helix | 137 | 1 | |
| α-helix | 138-146 | 9 | |
| β-strand | 157-160 | 4 | 1 |
| α-helix | 165-174 | 10 | |
| α-helix | 183-193 | 11 | |
| β-strand | 197-199 | 3 | 1 |
| α-helix | 200-207 | 8 | |
| α-helix | 229-235 | 7 | |
| α-helix | 242-245 | 4 | |
| α-helix | 247-264 | 18 | |
| β-strand | 268 | 1 | 3 |
| β-strand | 274 | 1 | 3 |
| α-helix | 275-278 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-14 | 4 | |
| β-strand | 17-19 | 3 | 4 |
| α-helix | 21-23 | 3 | |
| α-helix | 24-35 | 12 | |
| β-strand | 40-48 | 9 | 4 |
| α-helix | 63-72 | 10 | |
| α-helix | 73-75 | 3 | |
| β-strand | 77-86 | 10 | 4 |
| β-strand | 99-103 | 5 | 4 |
| β-strand | 104 | 1 | 5 |
| α-helix | 115-124 | 10 | |
| α-helix | 128-134 | 7 | |
| α-helix | 135 | 1 | |
| β-strand | 136 | 1 | 5 |
| α-helix | 137 | 1 | |
| α-helix | 138-146 | 9 | |
| β-strand | 157-160 | 4 | 4 |
| α-helix | 164-173 | 10 | |
| α-helix | 183-193 | 11 | |
| β-strand | 197-199 | 3 | 4 |
| α-helix | 200-206 | 7 | |
| α-helix | 229-236 | 8 | |
| α-helix | 242-245 | 4 | |
| α-helix | 247-264 | 18 | |
| β-strand | 268 | 1 | 6 |
| β-strand | 274 | 1 | 6 |
| α-helix | 275-278 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| POP2 | A, B | protein | 289 | SACCHAROMYCES CEREVISIAE | P39008 (AlphaFold model) |
>1UOC_1 POP2 (chains A, B) GAMPPIFLPPPNYLFVRDVWKSNLYSEFAVIRQLVSQYNHVSISTEFVGTLARPIGTFRS KVDYHYQTMRANVDFLNPIQLGLSLSDANGNKPDNGPSTWQFNFEFDPKKEIMSTESLEL LRKSGINFEKHENLGIDVFEFSQLLMDSGLMMDDSVTWITYHAAYDLGFLINILMNDSMP NNKEDFEWWVHQYMPNFYDLNLVYKIIQEFKNPQLQQSSQQQQQQQYSLTTLADELGLPR FSIFTTTGGQSLLMLLSFCQLSKLSMHKFPNGTDFAKYQGVIYGIDGDQ
X-Ray Structure and Activity of the Yeast Pop2 Protein: A Nuclease Subunit of the Mrna Deadenylase Complex. Thore, S., Mauxion, F., Seraphin, B. et al. EMBO Rep (2003) 4:1150. DOI 10.1038/SJ.EMBOR.7400020 · PubMed
Other PDB entries of the same protein (UniProt P39008 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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