the SNL domain of SidC. Determined by X-ray diffraction at 2.59 Å resolution. Released 2 Jul 2014.
Explore 4TRG in 3D Show helices and sheets RCSB PDB PDBe
4TRG contains 67 α-helices and 40 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 | 9-11 | 3 | |
| β-strand | 20-22 | 3 | 1 |
| β-strand | 28-30 | 3 | 1 |
| β-strand | 31-36 | 6 | 2 |
| β-strand | 37 | 1 | 3 |
| β-strand | 40 | 1 | 4 |
| β-strand | 41 | 1 | 3 |
| α-helix | 45-47 | 3 | |
| α-helix | 50-57 | 8 | |
| β-strand | 59-61 | 3 | 5 |
| β-strand | 64-66 | 3 | 5 |
| α-helix | 69-88 | 20 | |
| α-helix | 90-93 | 4 | |
| α-helix | 99-124 | 26 | |
| α-helix | 134-137 | 4 | |
| α-helix | 141-144 | 4 | |
| α-helix | 145-152 | 8 | |
| β-strand | 157-161 | 5 | 4 |
| β-strand | 178 | 1 | 4 |
| α-helix | 183 | 1 | |
| β-strand | 184 | 1 | 6 |
| α-helix | 185 | 1 | |
| α-helix | 186-188 | 3 | |
| α-helix | 195 | 1 | |
| β-strand | 196 | 1 | 6 |
| α-helix | 197-198 | 2 | |
| α-helix | 202-210 | 9 | |
| α-helix | 216-217 | 2 | |
| β-strand | 218-219 | 2 | 7 |
| α-helix | 225-234 | 10 | |
| α-helix | 248-268 | 21 | |
| α-helix | 272-276 | 5 | |
| β-strand | 281 | 1 | 8 |
| β-strand | 287 | 1 | 8 |
| α-helix | 290-291 | 2 | |
| α-helix | 292-296 | 5 | |
| α-helix | 306-317 | 12 | |
| α-helix | 320-323 | 4 | |
| α-helix | 324-329 | 6 | |
| β-strand | 337-338 | 2 | 7 |
| α-helix | 341-364 | 24 | |
| α-helix | 372-377 | 6 | |
| α-helix | 381-394 | 14 | |
| α-helix | 399-408 | 10 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-421 | 3 | |
| α-helix | 422-439 | 18 | |
| β-strand | 447-451 | 5 | 4 |
| β-strand | 459-462 | 4 | 2 |
| β-strand | 465-469 | 5 | 2 |
| α-helix | 470-477 | 8 | |
| α-helix | 485-487 | 3 | |
| α-helix | 490-495 | 6 | |
| β-strand | 501 | 1 | 2 |
| α-helix | 507-510 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-22 | 3 | 9 |
| β-strand | 28-30 | 3 | 9 |
| β-strand | 31-36 | 6 | 10 |
| β-strand | 37 | 1 | 11 |
| β-strand | 40 | 1 | 12 |
| β-strand | 41 | 1 | 11 |
| α-helix | 45-47 | 3 | |
| α-helix | 50-57 | 8 | |
| β-strand | 59-61 | 3 | 13 |
| β-strand | 64-66 | 3 | 13 |
| α-helix | 69-93 | 25 | |
| α-helix | 99-124 | 26 | |
| α-helix | 133-137 | 5 | |
| α-helix | 145-152 | 8 | |
| β-strand | 157-161 | 5 | 12 |
| β-strand | 178 | 1 | 12 |
| α-helix | 183 | 1 | |
| β-strand | 184 | 1 | 14 |
| α-helix | 185 | 1 | |
| α-helix | 186-188 | 3 | |
| α-helix | 195 | 1 | |
| β-strand | 196 | 1 | 14 |
| α-helix | 197-198 | 2 | |
| α-helix | 202-210 | 9 | |
| α-helix | 217 | 1 | |
| β-strand | 218-219 | 2 | 15 |
| α-helix | 225-234 | 10 | |
| α-helix | 248-268 | 21 | |
| α-helix | 272-276 | 5 | |
| β-strand | 281 | 1 | 16 |
| β-strand | 287 | 1 | 16 |
| α-helix | 290-291 | 2 | |
| α-helix | 292-296 | 5 | |
| α-helix | 306-317 | 12 | |
| α-helix | 320-323 | 4 | |
| α-helix | 324-329 | 6 | |
| β-strand | 337-338 | 2 | 15 |
| α-helix | 341-364 | 24 | |
| α-helix | 372-377 | 6 | |
| α-helix | 381-395 | 15 | |
| α-helix | 399-408 | 10 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-421 | 3 | |
| α-helix | 422-439 | 18 | |
| β-strand | 447-451 | 5 | 12 |
| β-strand | 459-462 | 4 | 10 |
| β-strand | 465-469 | 5 | 10 |
| α-helix | 470-477 | 8 | |
| α-helix | 485-487 | 3 | |
| α-helix | 490-495 | 6 | |
| β-strand | 501-502 | 2 | 10 |
| α-helix | 507-514 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SidC | A, B | protein | 542 | Legionella pneumophila | Q6RCR4 (AlphaFold model) |
>4TRG_1 SidC (chains A, B) MVINMVDVIKFKEPERCDYLYVDENNKVHILLPIVGGDEIGLDNTCQTAVELITFFYGSA HSGVTKYSAEHQLSEYKRQLEEDIKAINSQKKISPHAYDDLLKEKIERLQQIEKYIELIQ VLKKQYDEQNDIRQLRTGGIPQLPSGVKEIIKSSENAFAVRLSPYDNDKFTRFDDPLFNV KRNISKYDTPSRQAPIPIYEGLGYRLRSTLFPEDKTPTPINKKSLRDKVKSTVLSHYKDE DRIDGEKKDEKLNELITNLQNELVKELVKSDPQYSKLSLSKDPRGKEINYDYLVNSLMLV DNDSEIGDWIDTILDATVDSTVWVAQASSPFYDGAKEISSDRDADKISIRVQYLLAEANI YCKTNKLSDANFGEFFDKEPHATEIAKRVKEGFTQGADIEPIIYDYINSNHAELGLKSPL TGKQQQEITDKFTKHYNTIKESPHFDEFFVADPDKKGNIFSHQGRISCHFLDFFTRQTKG KHPLGDLASHQEALQEGTSNRLHHKNEVVAQGYEKLDQFKKEVVKLLAENKPKELLDYLV AT
| ID | Name | Formula | Copies |
|---|---|---|---|
| HG | Mercury (II) ion | Hg | 4 |
The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling. Hsu, F., Luo, X., Qiu, J. et al. Proc Natl Acad Sci U S A (2014) 111:10538-10543. DOI 10.1073/pnas.1402605111 · PubMed
Other PDB entries of the same protein (UniProt Q6RCR4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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