Crystal structure of IpgC in complex with an IpaB peptide. Determined by X-ray diffraction at 2.65 Å resolution. Released 21 Apr 2010.
Explore 3GZ2 in 3D Show helices and sheets RCSB PDB PDBe
3GZ2 contains 18 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 | 11-20 | 10 | |
| α-helix | 25-28 | 4 | |
| α-helix | 33-48 | 16 | |
| α-helix | 52-65 | 14 | |
| α-helix | 70-83 | 14 | |
| α-helix | 86-99 | 14 | |
| α-helix | 105-116 | 12 | |
| α-helix | 120-133 | 14 | |
| α-helix | 137-150 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-21 | 10 | |
| α-helix | 25-28 | 4 | |
| α-helix | 35-48 | 14 | |
| 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 | 137-150 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperone protein ipgC | A, B | protein | 151 | Shigella flexneri | P0A2U4 (AlphaFold model) |
| Invasin ipaB | P | protein | 78 | Shigella flexneri | P18011 (AlphaFold model) |
>3GZ2_1 Chaperone protein ipgC (chains A, B) GSLNITENESISTAVIDAINSGATLKDINAIPDDMMDDIYSYAYDFYNKGRIEEAEVFFR FLCIYDFYNVDYIMGLAAIYQIKEQFQQAADLYAVAFALGKNDYTPVFHTGQCQLRLKAP LKAKECFELVIQHSNDEKLKIKAQSYLDAIQ
>3GZ2_2 Invasin ipaB (chains P) MGSSHHHHHHSSGLVPRGSHMILTSTELGDNTIQAANDAANKLFSLTIADLTANQNINTT NAHSTSNILIPELKAPKS
Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB. Lokareddy, R.K., Lunelli, M., Eilers, B. et al. J Biol Chem (2010) 285:39965-39975. DOI 10.1074/jbc.M110.135616 · 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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