Chaperone Spy bound to Im7 (Im7 un-modeled). Determined by X-ray diffraction at 1.87 Å resolution. Released 16 Aug 2017.
Explore 5WO3 in 3D Show helices and sheets RCSB PDB PDBe
5WO3 contains 10 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 | 29-32 | 4 | |
| α-helix | 36-45 | 10 | |
| α-helix | 58-68 | 11 | |
| α-helix | 75-83 | 9 | |
| α-helix | 86-106 | 21 | |
| α-helix | 109-119 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-47 | 12 | |
| α-helix | 59-68 | 10 | |
| α-helix | 75-104 | 30 | |
| α-helix | 109-121 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Periplasmic chaperone Spy | A, B | protein | 97 | Escherichia coli | P77754 (AlphaFold model) |
>5WO3_1 Periplasmic chaperone Spy (chains A, B) SFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEE QRKANMLALMETQNKIYNILTPEQKKQFNANFEKRLT
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 12 |
Water and common crystallization additives (CL, IMD) are not listed.
Visualizing chaperone-assisted protein folding. Horowitz, S., Salmon, L., Koldewey, P. et al. Nat Struct Mol Biol (2016) 23:691-697. DOI 10.1038/nsmb.3237 · PubMed
Other PDB entries of the same protein (UniProt P77754 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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