1RPO: Rop protein

Restored heptad pattern continuity does not alter the folding of a 4-alpha-helical bundle. Determined by X-ray diffraction at 1.4 Å resolution. Released 14 Feb 1995.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Escherichia coli
Chains
1
Atoms
622
Mol. weight
7.38 kDa
Released
14 Feb 1995

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

Secondary structure: helices and β-sheets

1RPO contains 3 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.

Chain A: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-2826
α-helix30-334
α-helix34-5825

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rop proteinAprotein65Escherichia coliP03051 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RPO_1 ROP PROTEIN (chains A)
MTKQEKTALNMARFIRSQTLTLLEKLNELADAADEQADICESLHDHADELYRSCLARFGD
DGENL

Primary citation

Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle. Vlassi, M., Steif, C., Weber, P. et al. Nat Struct Biol (1994) 1:706-716. DOI 10.1038/nsb1094-706 · PubMed

Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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