3WRP: Trp repressor

Flexibility of the DNA-binding domains of trp repressor. Determined by X-ray diffraction at 1.8 Å resolution. Released 16 Apr 1988.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Escherichia coli
Chains
1
Atoms
884
Mol. weight
12.37 kDa
Released
16 Apr 1988

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

Secondary structure: helices and β-sheets

3WRP contains 6 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix12-3019
α-helix35-428
α-helix45-6319
α-helix68-758
α-helix79-9012
α-helix94-10411

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Trp repressorAprotein108Escherichia coliP0A881 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3WRP_1 TRP REPRESSOR (chains A)
MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEE
LLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD

Primary citation

Flexibility of the DNA-binding domains of trp repressor. Lawson, C.L., Zhang, R.G., Schevitz, R.W. et al. Proteins (1988) 3:18-31. DOI 10.1002/prot.340030103 · PubMed

Other PDB entries of the same protein (UniProt P0A881 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3WRP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.