The structure of COLE1 rop in solution. Determined by solution NMR. Released 31 Jan 1994.
Explore 1RPR in 3D Show helices and sheets RCSB PDB PDBe
1RPR contains 4 α-helices and 0 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 | 4-28 | 25 | |
| α-helix | 32-55 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-28 | 26 | |
| α-helix | 32-55 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ROP | A, B | protein | 63 | Escherichia coli | P03051 (AlphaFold model) |
>1RPR_1 ROP (chains A, B) MTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDG ENL
The structure of ColE1 rop in solution. Eberle, W., Pastore, A., Sander, C. et al. J Biomol NMR (1991) 1:71-82. DOI 10.1007/BF01874570 · PubMed
Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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