Crystal Structure of Type-III Secretion Chaperone IpgC from Shigella flexneri (residues 10-155). Determined by X-ray diffraction at 3.3 Å resolution. Released 25 Aug 2010.
Explore 3KS2 in 3D Show helices and sheets RCSB PDB PDBe
3KS2 contains 126 α-helices and 0 β-strands across 18 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 | 33-48 | 16 | |
| α-helix | 52-65 | 14 | |
| α-helix | 70-82 | 13 | |
| α-helix | 86-98 | 13 | |
| α-helix | 105-116 | 12 | |
| α-helix | 120-133 | 14 | |
| α-helix | 137-151 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperone protein ipgC | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | protein | 151 | Shigella flexneri | P0A2U4 (AlphaFold model) |
>3KS2_1 Chaperone protein ipgC (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R) GSTGSSISTAVIDAINSGATLKDINAIPDDMMDDIYSYAYDFYNKGRIEEAEVFFRFLCI YDFYNVDYIMGLAAIYQIKEQFQQAADLYAVAFALGKNDYTPVFHTGQCQLRLKAPLKAK ECFELVIQHSNDEKLKIKAQSYLDAIQDIKE
Evidence for alternative quaternary structure in a bacterial Type III secretion system chaperone. Barta, M.L., Zhang, L., Picking, W.L. et al. BMC Struct Biol (2010) 10:21-21. DOI 10.1186/1472-6807-10-21 · PubMed
Other PDB entries of the same protein (UniProt P0A2U4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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