Crystal structure of ExoT (residues 28 -77)- SpcS complex from Pseudomonas aeruginosa at 2.1 angstrom. Determined by X-ray diffraction at 2.1 Å resolution. Released 5 Feb 2014.
Explore 4JMF in 3D Show helices and sheets RCSB PDB PDBe
4JMF contains 13 α-helices and 13 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 |
|---|---|---|---|
| β-strand | 29-32 | 4 | 1 |
| α-helix | 33-35 | 3 | |
| α-helix | 36-41 | 6 | |
| α-helix | 53-57 | 5 | |
| β-strand | 59-61 | 3 | 2 |
| α-helix | 66-76 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-22 | 4 | |
| β-strand | 28-32 | 5 | 2 |
| β-strand | 35-41 | 7 | 2 |
| β-strand | 46-53 | 8 | 2 |
| β-strand | 62 | 1 | 1 |
| β-strand | 75-78 | 4 | 2 |
| β-strand | 85-92 | 8 | 2 |
| α-helix | 93-95 | 3 | |
| α-helix | 98-114 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-21 | 3 | |
| β-strand | 28-32 | 5 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 46-52 | 7 | 1 |
| α-helix | 61-64 | 4 | |
| β-strand | 75-78 | 4 | 1 |
| β-strand | 85-92 | 8 | 1 |
| α-helix | 93-95 | 3 | |
| α-helix | 98-114 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exoenzyme T | A | protein | 50 | Pseudomonas aeruginosa | Q9I788 (AlphaFold model) |
| Probable chaperone | B, C | protein | 116 | Pseudomonas aeruginosa | G3XD93 (AlphaFold model) |
>4JMF_1 Exoenzyme T (chains A) EARQVATPREAQQLAQRQEAPKGEGLLSRLGAALARPFVAIIEWLGKLLG
>4JMF_2 Probable chaperone (chains B, C) MNPLYRAAIHQLFLALDLPTPNDEESVLSLQVGPHLCHLAEHPTDHLLMFTRLEGQGDAT ANEQNLFSQDPCKPILGRDPESGERLLWNRQPLQLLDRAQIHHQLEQLVAAAEELR
Interfacial residues of SpcS chaperone affects binding of effector toxin ExoT in Pseudomonas aeruginosa: novel insights from structural and computational studies. Dey, S., Datta, S. FEBS J (2014) 281:1267-1280. DOI 10.1111/febs.12704 · PubMed
Other PDB entries of the same protein (UniProt Q9I788 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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