Solution structure of a dimer of lac repressor DNA-binding domain complexed to its natural operator O1. Determined by solution NMR. Released 26 Jun 2002.
Explore 1L1M in 3D Show helices and sheets RCSB PDB PDBe
1L1M contains 8 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-13 | 8 | |
| α-helix | 17-25 | 9 | |
| α-helix | 32-44 | 13 | |
| α-helix | 51-57 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-13 | 8 | |
| α-helix | 17-24 | 8 | |
| α-helix | 32-44 | 13 | |
| α-helix | 51-57 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*gp*ap*ap*tp*tp*gp*tp*gp*ap*gp*cp*gp*gp*ap*tp*ap*ap*cp*ap*ap*tp*tp*t)-3' | C | DNA | 23 | ||
| 5'-d(*ap*ap*ap*tp*tp*gp*tp*tp*ap*tp*cp*cp*gp*cp*tp*cp*ap*cp*ap*ap*tp*tp*c)-3' | D | DNA | 23 | ||
| Lactose operon repressor | A, B | protein | 62 | Escherichia coli | P03023 (AlphaFold model) |
>1L1M_1 5'-D(*GP*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*GP*GP*AP*TP*AP*AP*CP*AP*AP*TP*TP*T)-3' (chains C) GAATTGTGAGCGGATAACAATTT
>1L1M_2 5'-D(*AP*AP*AP*TP*TP*GP*TP*TP*AP*TP*CP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*TP*C)-3' (chains D) AAATTGTTATCCGCTCACAATTC
>1L1M_3 Lactose operon repressor (chains A, B) MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRCAQQLAGKQ SL
Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. Kalodimos, C.G., Bonvin, A.M., Salinas, R.K. et al. EMBO J (2002) 21:2866-2876. DOI 10.1093/emboj/cdf318 · PubMed
Other PDB entries of the same protein (UniProt P03023 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1L1M 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.