3K79: C38A, C52V Cysteine-Free Variant of Rop

C38A, C52V Cysteine-Free Variant of Rop (Rom). Determined by X-ray diffraction at 1.96 Å resolution. Released 2 Feb 2010.

Method
X-ray diffraction
Resolution
1.96 Å
Organism
Escherichia coli
Chains
1
Atoms
523
Mol. weight
7.13 kDa
Released
2 Feb 2010

Explore 3K79 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2-2827
α-helix32-5625

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulatory protein ropAprotein63Escherichia coliP03051 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3K79_1 Regulatory protein rop (chains A)
GTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADIAESLHDHADELYRSVLARFGDDG
ENL

Primary citation

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:

Browse structure collections

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