Structure of the COL*E1 rop protein at 1.7 Å resolution. Determined by X-ray diffraction at 1.7 Å resolution. Released 15 Jul 1992.
Explore 1ROP in 3D Show helices and sheets RCSB PDB PDBe
1ROP contains 2 α-helices and 0 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 | 3-28 | 26 | |
| α-helix | 32-55 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rop protein | A | protein | 63 | Escherichia coli | P03051 (AlphaFold model) |
>1ROP_1 ROP PROTEIN (chains A) MTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDG ENL
Structure of the ColE1 rop protein at 1.7 A resolution. Banner, D.W., Kokkinidis, M., Tsernoglou, D. J Mol Biol (1987) 196:657-675. DOI 10.1016/0022-2836(87)90039-8 · PubMed
Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1ROP is part of these collections:
MolViewer shows 1ROP 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.