1QX8: Five-residue deletion mutant of the Rop protein

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.

Method
X-ray diffraction
Resolution
2.02 Å
Organism
Escherichia coli
Chains
2
Atoms
869
Mol. weight
13.36 kDa
Released
28 Sept 2004

Explore 1QX8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix6-5045
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3-5048

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulatory protein ROPA, Bprotein58Escherichia coliP03051 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1QX8_1 Regulatory protein ROP (chains A, B)
MTKQEKTALNMARFIRSQTLTLLEKLNELADICESLHDHADELYRSCLARFGDDGENL

Primary citation

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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