C38A, C52V Cysteine-Free Variant of Rop (Rom). Determined by X-ray diffraction at 1.96 Å resolution. Released 2 Feb 2010.
Explore 3K79 in 3D Show helices and sheets RCSB PDB PDBe
3K79 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 | 2-28 | 27 | |
| α-helix | 32-56 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory protein rop | A | protein | 63 | Escherichia coli | P03051 (AlphaFold model) |
>3K79_1 Regulatory protein rop (chains A) GTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADIAESLHDHADELYRSVLARFGDDG ENL
Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics. Hari, S.B., Byeon, C., Lavinder, J.J. et al. Protein Sci (2010) 19:670-679. DOI 10.1002/pro.342 · 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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