Pi-scei, a homing endonuclease with protein splicing activity. Determined by X-ray diffraction at 2.4 Å resolution. Released 8 Apr 1998.
Explore 1VDE in 3D Show helices and sheets RCSB PDB PDBe
1VDE contains 32 α-helices and 72 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 |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| β-strand | 7-9 | 3 | 2 |
| β-strand | 10 | 1 | 3 |
| β-strand | 15-17 | 3 | 2 |
| α-helix | 18-20 | 3 | |
| β-strand | 26-28 | 3 | 3 |
| α-helix | 29 | 1 | |
| β-strand | 34-36 | 3 | 3 |
| β-strand | 37-39 | 3 | 4 |
| β-strand | 42-52 | 11 | 1 |
| β-strand | 57 | 1 | 5 |
| α-helix | 67 | 1 | |
| β-strand | 68 | 1 | 5 |
| β-strand | 72-76 | 5 | 1 |
| α-helix | 79 | 1 | |
| β-strand | 80-86 | 7 | 6 |
| β-strand | 89-90 | 2 | 7 |
| β-strand | 104-113 | 10 | 7 |
| β-strand | 119-128 | 10 | 7 |
| α-helix | 138-148 | 11 | |
| β-strand | 154-160 | 7 | 6 |
| α-helix | 161-166 | 6 | |
| α-helix | 169-174 | 6 | |
| β-strand | 176-179 | 4 | 6 |
| α-helix | 188-195 | 8 | |
| α-helix | 204-218 | 15 | |
| β-strand | 219 | 1 | 8 |
| β-strand | 225-229 | 5 | 8 |
| α-helix | 233-245 | 13 | |
| β-strand | 248-254 | 7 | 8 |
| β-strand | 261-268 | 8 | 8 |
| α-helix | 269 | 1 | |
| α-helix | 285-292 | 8 | |
| β-strand | 296-297 | 2 | 9 |
| β-strand | 300-301 | 2 | 9 |
| α-helix | 305-309 | 5 | |
| α-helix | 312-326 | 15 | |
| β-strand | 327-330 | 4 | 10 |
| β-strand | 332 | 1 | 11 |
| β-strand | 334 | 1 | 11 |
| β-strand | 336-341 | 6 | 10 |
| α-helix | 344-356 | 13 | |
| β-strand | 360-366 | 7 | 10 |
| β-strand | 380-386 | 7 | 10 |
| α-helix | 388-395 | 8 | |
| α-helix | 406-408 | 3 | |
| β-strand | 417-419 | 3 | 6 |
| β-strand | 421-432 | 12 | 1 |
| β-strand | 435-436 | 2 | 4 |
| β-strand | 443-445 | 3 | 12 |
| β-strand | 446 | 1 | 2 |
| β-strand | 450 | 1 | 6 |
| β-strand | 451-453 | 3 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 13 |
| β-strand | 7-9 | 3 | 14 |
| β-strand | 10 | 1 | 15 |
| β-strand | 15-17 | 3 | 14 |
| α-helix | 18-20 | 3 | |
| β-strand | 26-28 | 3 | 15 |
| β-strand | 34-36 | 3 | 15 |
| β-strand | 37-39 | 3 | 16 |
| β-strand | 42-44 | 3 | 13 |
| β-strand | 47-52 | 6 | 13 |
| β-strand | 72-76 | 5 | 13 |
| α-helix | 79 | 1 | |
| β-strand | 80-86 | 7 | 17 |
| β-strand | 89-90 | 2 | 18 |
| β-strand | 104-113 | 10 | 18 |
| β-strand | 119-128 | 10 | 18 |
| α-helix | 132-134 | 3 | |
| α-helix | 137-148 | 12 | |
| β-strand | 154-160 | 7 | 17 |
| α-helix | 161-166 | 6 | |
| α-helix | 169-174 | 6 | |
| β-strand | 176-179 | 4 | 17 |
| α-helix | 188-194 | 7 | |
| α-helix | 205-218 | 14 | |
| β-strand | 219 | 1 | 19 |
| β-strand | 225-226 | 2 | 19 |
| α-helix | 235-245 | 11 | |
| β-strand | 248-252 | 5 | 19 |
| β-strand | 264-268 | 5 | 19 |
| α-helix | 285-293 | 9 | |
| β-strand | 296 | 1 | 20 |
| β-strand | 301 | 1 | 20 |
| α-helix | 306-309 | 4 | |
| α-helix | 312-326 | 15 | |
| β-strand | 327-330 | 4 | 21 |
| β-strand | 332 | 1 | 22 |
| β-strand | 334 | 1 | 22 |
| β-strand | 336-341 | 6 | 21 |
| α-helix | 344-357 | 14 | |
| β-strand | 360-366 | 7 | 21 |
| β-strand | 380-386 | 7 | 21 |
| α-helix | 389-395 | 7 | |
| α-helix | 406-408 | 3 | |
| β-strand | 417-419 | 3 | 17 |
| β-strand | 421-425 | 5 | 13 |
| β-strand | 430-432 | 3 | 13 |
| β-strand | 435-436 | 2 | 16 |
| β-strand | 443-445 | 3 | 23 |
| β-strand | 446 | 1 | 14 |
| β-strand | 450 | 1 | 17 |
| β-strand | 451-453 | 3 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pi-scei | A, B | protein | 454 | Saccharomyces cerevisiae | P17255 (AlphaFold model) |
>1VDE_1 PI-SCEI (chains A, B) CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHK SDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIV ELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYA PILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVT EYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGV KNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLV VSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFY FELQELKEDDYYGITLSDDSDHQFLLANQVVVHN
Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Duan, X., Gimble, F.S., Quiocho, F.A. Cell (1997) 89:555-564. DOI 10.1016/S0092-8674(00)80237-8 · PubMed
Other PDB entries of the same protein (UniProt P17255 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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