Structure of Salmonella SipA residues 48-264. Determined by X-ray diffraction at 2.0 Å resolution. Released 21 Mar 2006.
Explore 2FM9 in 3D Show helices and sheets RCSB PDB PDBe
2FM9 contains 12 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-53 | 3 | |
| α-helix | 55-68 | 14 | |
| α-helix | 73-82 | 10 | |
| α-helix | 86-105 | 20 | |
| α-helix | 110-130 | 21 | |
| α-helix | 146-165 | 20 | |
| α-helix | 168-178 | 11 | |
| α-helix | 179-183 | 5 | |
| α-helix | 184-195 | 12 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-227 | 27 | |
| α-helix | 245-258 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell invasion protein sipA | A | protein | 215 | Salmonella typhimurium | P0CL52 (AlphaFold model) |
>2FM9_1 Cell invasion protein sipA (chains A) PQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSD SPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTG GELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQK LTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPA
A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Lilic, M., Vujanac, M., Stebbins, C.E. Mol Cell (2006) 21:653-664. DOI 10.1016/j.molcel.2006.01.026 · PubMed
Other PDB entries of the same protein (UniProt P0CL52 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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