E. coli trp repressor, tetragonal crystal form. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 May 2006.
Explore 1ZT9 in 3D Show helices and sheets RCSB PDB PDBe
1ZT9 contains 24 α-helices and 0 β-strands across 4 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 | 9-31 | 23 | |
| α-helix | 35-42 | 8 | |
| α-helix | 45-63 | 19 | |
| α-helix | 68-75 | 8 | |
| α-helix | 79-91 | 13 | |
| α-helix | 94-104 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trp operon repressor | A, B, D, E | protein | 107 | Escherichia coli | P0A881 (AlphaFold model) |
>1ZT9_1 Trp operon repressor (chains A, B, D, E) AQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEEL LRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD
| ID | Name | Formula | Copies |
|---|---|---|---|
| TRP | Tryptophan | C11 H12 N2 O2 | 4 |
Water and common crystallization additives (SO4) are not listed.
Two association modes for E. coli trp repressor dimer-dimer interactions. Lawson, C.L., Chin, A.S., Benoff, B. et al. To be published.
Other PDB entries of the same protein (UniProt P0A881 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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