Solution structure of the Escherichia coli TolA C-terminal domain. Determined by solution NMR. Released 15 Feb 2005.
Explore 1S62 in 3D Show helices and sheets RCSB PDB PDBe
1S62 contains 3 α-helices and 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-28 | 15 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 53-59 | 7 | 2 |
| α-helix | 64-75 | 12 | |
| α-helix | 85-91 | 7 | |
| β-strand | 97 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TolA protein | A | protein | 106 | Escherichia coli | P19934 (AlphaFold model) |
>1S62_1 TolA protein (chains A) AEFGNTKNNGASGADINNYAGQIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPE GGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKPHHHHHH
Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain. Deprez, C., Lloubes, R., Gavioli, M. et al. J Mol Biol (2005) 346:1047-1057. DOI 10.1016/j.jmb.2004.12.028 · PubMed
Other PDB entries of the same protein (UniProt P19934 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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