Crystal structure of an effector from Chromobacterium violaceum in complex with ubiquitin. Determined by X-ray diffraction at 1.85 Å resolution. Released 22 Nov 2023.
Explore 8HTD in 3D Show helices and sheets RCSB PDB PDBe
8HTD contains 16 α-helices and 21 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 | 46-57 | 12 | |
| β-strand | 62-67 | 6 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 73-78 | 6 | |
| α-helix | 79-86 | 8 | |
| β-strand | 96-98 | 3 | 2 |
| β-strand | 99-101 | 3 | 1 |
| β-strand | 107 | 1 | 3 |
| β-strand | 117-121 | 5 | 1 |
| β-strand | 126-131 | 6 | 2 |
| β-strand | 157 | 1 | 4 |
| α-helix | 159-166 | 8 | |
| α-helix | 169-173 | 5 | |
| α-helix | 181-187 | 7 | |
| α-helix | 191-193 | 3 | |
| β-strand | 194 | 1 | 4 |
| β-strand | 196 | 1 | 2 |
| α-helix | 199-212 | 14 | |
| β-strand | 216 | 1 | 3 |
| α-helix | 217-219 | 3 | |
| β-strand | 220-224 | 5 | 2 |
| α-helix | 227-229 | 3 | |
| β-strand | 230-234 | 5 | 1 |
| α-helix | 240-255 | 16 | |
| β-strand | 262-266 | 5 | 1 |
| β-strand | 269-273 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 5 |
| β-strand | 12-16 | 5 | 5 |
| β-strand | 22 | 1 | 6 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 5 |
| β-strand | 48-49 | 2 | 5 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 6 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAD(+)--protein-threonine ADP-ribosyltransferase | A | protein | 233 | Chromobacterium violaceum ATCC 12472 | Q7NY09 (AlphaFold model) |
| Ubiquitin | B | protein | 76 | Saccharomyces cerevisiae S288C | P0CH08 (AlphaFold model) |
>8HTD_1 NAD(+)--protein-threonine ADP-ribosyltransferase (chains A) SNRQEKLAQLMRQFESGGLYLRTVSDHRDEFENTFMPKLDACLGHGCDERYWSSATFIQQ GLNGKVHDPHADRTGLIISADARLGGFSTFDAATANVPSGLEPSQYFPGQFPKFDMMGAY QATWNEDIFSVDATAVSEQQMDELGIPDEYRSVFDFDRIQEKMAQPRLAGREVEPTEAKI CYQPKDVLGIYVDVDSPASQSKARELQQAMREQGFDLPFIAYRGGAAQELASV
>8HTD_2 Ubiquitin (chains B) MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs. Tan, J., Xu, Y., Wang, X. et al. Nat Chem Biol (2024) 20:463-472. DOI 10.1038/s41589-023-01475-3 · PubMed
Other PDB entries of the same protein (UniProt Q7NY09 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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