2OZ9: Trp operon repressor

E. coli TRP holorepressor, orthorhombic crystal form. Determined by X-ray diffraction at 1.65 Å resolution. Released 6 Mar 2007.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Escherichia coli
Chains
1
Atoms
934
Mol. weight
12.56 kDa
Ligands
TRP
Released
6 Mar 2007

Explore 2OZ9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OZ9 contains 7 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 R: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-3123
α-helix35-428
α-helix45-6319
α-helix68-758
α-helix79-9113
α-helix94-10411
α-helix106-1072

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Trp operon repressorRprotein107Escherichia coliP0A881 (AlphaFold model)
Sequence of entity 1 (R), FASTA
>2OZ9_1 Trp operon repressor (chains R)
AQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEEL
LRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD

Ligands and cofactors

IDNameFormulaCopies
TRPTryptophanC11 H12 N2 O21

Water and common crystallization additives (SO4, NA) are not listed.

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

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