Tryptophan Repressor TrpR from E.coli with 3-Indolepropionic acid. Determined by X-ray diffraction at 2.13 Å resolution. Released 27 Mar 2019.
Explore 6F7F in 3D Show helices and sheets RCSB PDB PDBe
6F7F 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-32 | 24 | |
| 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 |
| 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 | 79-90 | 12 | |
| α-helix | 94-103 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trp operon repressor | A, B, C, D | protein | 103 | Escherichia coli | P0A881 (AlphaFold model) |
>6F7F_1 Trp operon repressor (chains A, B, C, D) QSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLR GEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLK
| ID | Name | Formula | Copies |
|---|---|---|---|
| IOP | Indolylpropionic acid | C11 H11 N O2 | 4 |
Tryptophan Repressor TrpR: A study of ligand binding specificity. Stiel, A.C., Shanmugaratnam, S., Hocker, B. 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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