Crystal structure of pi-scei in C2 space group. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Dec 1999.
Explore 1DFA in 3D Show helices and sheets RCSB PDB PDBe
1DFA contains 14 α-helices and 32 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 |
|---|---|---|---|
| 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 | 27 | 1 | 3 |
| β-strand | 28 | 1 | 4 |
| β-strand | 34 | 1 | 4 |
| β-strand | 37 | 1 | 5 |
| β-strand | 43-52 | 10 | 1 |
| α-helix | 67-69 | 3 | |
| β-strand | 72-76 | 5 | 1 |
| β-strand | 80-86 | 7 | 6 |
| β-strand | 88-90 | 3 | 7 |
| β-strand | 105-113 | 9 | 7 |
| β-strand | 119-126 | 8 | 7 |
| β-strand | 154-160 | 7 | 6 |
| α-helix | 161-166 | 6 | |
| α-helix | 169-174 | 6 | |
| β-strand | 176 | 1 | 6 |
| β-strand | 177-179 | 3 | 8 |
| α-helix | 205-218 | 14 | |
| β-strand | 220 | 1 | 9 |
| β-strand | 223 | 1 | 9 |
| α-helix | 233-245 | 13 | |
| α-helix | 287-292 | 6 | |
| β-strand | 296 | 1 | 10 |
| β-strand | 301 | 1 | 10 |
| α-helix | 305-308 | 4 | |
| α-helix | 312-326 | 15 | |
| β-strand | 329-330 | 2 | 11 |
| β-strand | 336-341 | 6 | 11 |
| α-helix | 344-356 | 13 | |
| β-strand | 360-367 | 8 | 11 |
| α-helix | 371-373 | 3 | |
| β-strand | 379-386 | 8 | 11 |
| α-helix | 389-395 | 7 | |
| α-helix | 406-408 | 3 | |
| α-helix | 415-416 | 2 | |
| β-strand | 417-419 | 3 | 8 |
| β-strand | 421-431 | 11 | 1 |
| β-strand | 436 | 1 | 5 |
| β-strand | 443-445 | 3 | 12 |
| β-strand | 446 | 1 | 2 |
| β-strand | 450 | 1 | 8 |
| β-strand | 451-453 | 3 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pi-scei endonuclease | A | protein | 454 | Saccharomyces cerevisiae | P17255 (AlphaFold model) |
>1DFA_1 PI-SCEI ENDONUCLEASE (chains A) CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHK SDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIV ELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYA PILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVT EYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGV KNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLV VSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFY FELQELKEDDYYGITLSDDSDHQFLLANQVVVHN
Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking. Hu, D., Crist, M., Duan, X. et al. J Biol Chem (2000) 275:2705-2712. DOI 10.1074/jbc.275.4.2705 · PubMed
Other PDB entries of the same protein (UniProt P17255 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1DFA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.