Crystal structure of the S.cerevisiae Homing Endonuclease PI-SceI Domain I. Determined by X-ray diffraction at 1.35 Å resolution. Released 19 Sept 2002.
Explore 1GPP in 3D Show helices and sheets RCSB PDB PDBe
1GPP contains 8 α-helices and 26 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 | -1-2 | 3 | 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 |
| β-strand | 29 | 1 | 4 |
| β-strand | 34-36 | 3 | 3 |
| β-strand | 37-39 | 3 | 5 |
| β-strand | 42-52 | 11 | 1 |
| α-helix | 68-71 | 4 | |
| β-strand | 72-76 | 5 | 1 |
| α-helix | 79 | 1 | |
| β-strand | 80-86 | 7 | 6 |
| β-strand | 89-96 | 8 | 7 |
| β-strand | 99-113 | 15 | 7 |
| β-strand | 119-131 | 13 | 7 |
| α-helix | 132-134 | 3 | |
| α-helix | 137-148 | 12 | |
| 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 |
| β-strand | 182 | 1 | 9 |
| α-helix | 410-412 | 3 | |
| β-strand | 414 | 1 | 9 |
| β-strand | 417-419 | 3 | 8 |
| β-strand | 421-434 | 14 | 1 |
| β-strand | 435-436 | 2 | 5 |
| β-strand | 444-445 | 2 | 4 |
| β-strand | 446 | 1 | 2 |
| β-strand | 450 | 1 | 8 |
| β-strand | 451-452 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endonuclease pi-scei | A | protein | 237 | SACCHAROMYCES CEREVISIAE | P17255 (AlphaFold model) |
>1GPP_1 ENDONUCLEASE PI-SCEI (chains A) MHHHHHHGSACFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGSETMYSV VQKSQHRAHKSDSSREMPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMG QKKAPDGRIVELVKEVSKSYPVSEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSH VRKATYQTYAPIGAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVH
High Resolution Crystal Structure of Domain I of the Saccharomyces Cerevisiae Homing Endonuclease Pi-Scei. Werner, E., Wende, W., Pingoud, A. et al. Nucleic Acids Res (2002) 30:3962. DOI 10.1093/NAR/GKF523 · PubMed
Other PDB entries of the same protein (UniProt P17255 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1GPP 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.