1RPR: COLE1 rop in solution

The structure of COLE1 rop in solution. Determined by solution NMR. Released 31 Jan 1994.

Method
Solution NMR
Organism
Escherichia coli
Chains
2
Atoms
1,008
Mol. weight
14.47 kDa
Released
31 Jan 1994

Explore 1RPR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-2825
α-helix32-5524
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-2826
α-helix32-5524

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ROPA, Bprotein63Escherichia coliP03051 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1RPR_1 ROP (chains A, B)
MTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDG
ENL

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 1RPR 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.