Crystal structure of a five-residue deletion mutant of the Rop protein. Determined by X-ray diffraction at 2.02 Å resolution. Released 28 Sept 2004.
Explore 1QX8 in 3D Show helices and sheets RCSB PDB PDBe
1QX8 contains 2 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 | 6-50 | 45 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-50 | 48 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory protein ROP | A, B | protein | 58 | Escherichia coli | P03051 (AlphaFold model) |
>1QX8_1 Regulatory protein ROP (chains A, B) MTKQEKTALNMARFIRSQTLTLLEKLNELADICESLHDHADELYRSCLARFGDDGENL
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein. Glykos, N.M., Papanikolau, Y., Vlassi, M. et al. Biochemistry (2006) 45:10905-10919. DOI 10.1021/bi060833n · 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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