Crystal structure of Salmonella effector in complex with NAD and host co-factor ARF1. Determined by X-ray diffraction at 3.29 Å resolution. Released 15 Dec 2021.
Explore 7DN9 in 3D Show helices and sheets RCSB PDB PDBe
7DN9 contains 100 α-helices and 80 β-strands across 8 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 | 74-99 | 26 | |
| α-helix | 101-115 | 15 | |
| α-helix | 122-134 | 13 | |
| β-strand | 137-142 | 6 | 1 |
| α-helix | 149-154 | 6 | |
| β-strand | 157-158 | 2 | 2 |
| α-helix | 174-185 | 12 | |
| α-helix | 188-191 | 4 | |
| α-helix | 197-199 | 3 | |
| β-strand | 205 | 1 | 3 |
| β-strand | 211 | 1 | 3 |
| α-helix | 218-220 | 3 | |
| α-helix | 222 | 1 | |
| β-strand | 223-228 | 6 | 1 |
| α-helix | 238-240 | 3 | |
| β-strand | 243-247 | 5 | 1 |
| α-helix | 249-254 | 6 | |
| β-strand | 255-258 | 4 | 1 |
| α-helix | 271-273 | 3 | |
| β-strand | 275-276 | 2 | 1 |
| α-helix | 280-286 | 7 | |
| α-helix | 296-304 | 9 | |
| α-helix | 310-312 | 3 | |
| β-strand | 325-328 | 4 | 1 |
| β-strand | 332-333 | 2 | 2 |
| β-strand | 338-343 | 6 | 1 |
| α-helix | 352-366 | 15 | |
| β-strand | 371-373 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-24 | 7 | 4 |
| α-helix | 30-39 | 10 | |
| β-strand | 51-58 | 8 | 4 |
| β-strand | 61-68 | 8 | 4 |
| α-helix | 76-78 | 3 | |
| α-helix | 79-82 | 4 | |
| β-strand | 87-93 | 7 | 4 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-111 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 120-126 | 7 | 4 |
| α-helix | 136-143 | 8 | |
| α-helix | 145-147 | 3 | |
| β-strand | 153-157 | 5 | 4 |
| β-strand | 159 | 1 | 5 |
| β-strand | 164 | 1 | 5 |
| α-helix | 166-176 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-24 | 7 | 9 |
| α-helix | 30-39 | 10 | |
| β-strand | 51-58 | 8 | 9 |
| β-strand | 61-68 | 8 | 9 |
| α-helix | 76-78 | 3 | |
| α-helix | 79-82 | 4 | |
| β-strand | 87-93 | 7 | 9 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-111 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 120-126 | 7 | 9 |
| α-helix | 136-143 | 8 | |
| α-helix | 145-147 | 3 | |
| β-strand | 153-157 | 5 | 9 |
| β-strand | 159 | 1 | 10 |
| β-strand | 164 | 1 | 10 |
| α-helix | 166-175 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putative cytoplasmic protein | A, C, E, G | protein | 312 | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | Q8ZPY9 (AlphaFold model) |
| ADP-ribosylation factor 1 | B, D, F, H | protein | 165 | Homo sapiens | P84077 (AlphaFold model) |
>7DN9_1 Putative cytoplasmic protein (chains A, C, E, G) LSFDEVFCGLSNEERKKVYGRLFGKQVLAHIHSRCQRDADIIREKALRRISRECGAEIDC ALLLNKMVDILQNARLTINFNAAKIDFVSLLKNKEYLNSYALGCRPGDLPAYNVGRDSVE TKAFELEKLADSPYAPYGQTGGFSVAYTPNSRTFSTTSRPIYAALDFLNGENGGASAYGK SFFELNDNVKTNCTFSPFDIYGHRFGLDTSKLSTFWHMENLIASCQNDFFGYNCFKSLVK MAKDEKFLAHSNYGKGYEGNYIDAHIHGDVCLFRDIKHVYLSLQENSYSKSQLYDYAKQI NQALNRDCIILY
>7DN9_2 ADP-ribosylation factor 1 (chains B, D, F, H) EMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGLDKIRP LWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNA AEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 4 |
| MG | Magnesium ion | Mg | 4 |
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 4 |
ARF GTPases activate Salmonella effector SopF to ADP-ribosylate host V-ATPase and inhibit endomembrane damage-induced autophagy. Xu, Y., Cheng, S., Zeng, H. et al. Nat Struct Mol Biol (2022) 29:67-77. DOI 10.1038/s41594-021-00710-6 · PubMed
Other PDB entries of the same protein (UniProt Q8ZPY9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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