Structure of a Rom protein dimer at 1.55 angstrom resolution. Determined by X-ray diffraction at 1.55 Å resolution. Released 16 Oct 2007.
Explore 2IJK in 3D Show helices and sheets RCSB PDB PDBe
2IJK 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 | 3-28 | 26 | |
| α-helix | 32-56 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-28 | 27 | |
| α-helix | 32-56 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory protein rop | A, B | protein | 63 | Escherichia coli | P03051 (AlphaFold model) |
>2IJK_1 Regulatory protein rop (chains A, B) GTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDG ENL
New crystal structures of ColE1 Rom and variants resulting from mutation of a surface exposed residue: Implications for RNA-recognition. Struble, E.B., Ladner, J.E., Brabazon, D.M. et al. Proteins (2008) 72:761-768. DOI 10.1002/prot.21965 · 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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