Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Mar 2006.
Explore 2FM8 in 3D Show helices and sheets RCSB PDB PDBe
2FM8 contains 23 α-helices and 16 β-strands across 3 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 | 6-17 | 12 | |
| α-helix | 21-23 | 3 | |
| β-strand | 24 | 1 | 1 |
| β-strand | 32-37 | 6 | 1 |
| α-helix | 41-42 | 2 | |
| β-strand | 43-48 | 6 | 1 |
| β-strand | 51-57 | 7 | 1 |
| α-helix | 62-78 | 17 | |
| β-strand | 84 | 1 | 2 |
| α-helix | 85-87 | 3 | |
| β-strand | 90-94 | 5 | 1 |
| β-strand | 97-103 | 7 | 1 |
| β-strand | 104 | 1 | 2 |
| α-helix | 106-108 | 3 | |
| α-helix | 112-132 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-15 | 10 | |
| β-strand | 33-35 | 3 | 3 |
| β-strand | 43-48 | 6 | 3 |
| β-strand | 51-57 | 7 | 3 |
| α-helix | 62-68 | 7 | |
| α-helix | 70-77 | 8 | |
| β-strand | 84 | 1 | 4 |
| α-helix | 85-87 | 3 | |
| β-strand | 90-94 | 5 | 3 |
| β-strand | 97-103 | 7 | 3 |
| β-strand | 104 | 1 | 4 |
| α-helix | 106-108 | 3 | |
| α-helix | 112-133 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-29 | 4 | |
| β-strand | 31-37 | 7 | 1 |
| α-helix | 54-67 | 14 | |
| α-helix | 73-82 | 10 | |
| α-helix | 86-106 | 21 | |
| α-helix | 110-130 | 21 | |
| α-helix | 146-165 | 20 | |
| α-helix | 173-193 | 21 | |
| α-helix | 201-204 | 4 | |
| α-helix | 208-228 | 21 | |
| α-helix | 241-260 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Surface presentation of antigens protein spaK | A, B | protein | 135 | Salmonella typhimurium | P0A1N0 (AlphaFold model) |
| Cell invasion protein sipA | C | protein | 240 | Salmonella typhimurium | P0CL52 (AlphaFold model) |
>2FM8_1 Surface presentation of antigens protein spaK (chains A, B) MQHLDIAELVRSALEVSGCDPSLIGGIDSHSTIVLDLFALPSICISVKDDDVWIWAQLGA DSMVVLQQRAYEILMTIMEGCHFARGGQLLLGEQNGELTLKALVHPDFLSDGEKFSTALN GFYNYLEVFSRSLMR
>2FM8_2 Cell invasion protein sipA (chains C) QATNLAANLSAVRESATATLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTN SNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWL PETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPL TRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIP
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
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