Chromobacterium violaceum mono-ADP-ribosyltransferase CteC in complex with NAD+. Determined by X-ray diffraction at 1.87 Å resolution. Released 17 Jan 2024.
Explore 8UX2 in 3D Show helices and sheets RCSB PDB PDBe
8UX2 contains 45 α-helices and 42 β-strands across 3 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 | 39-42 | 4 | |
| 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 | 199-201 | 3 | |
| α-helix | 202-205 | 4 | |
| α-helix | 207-212 | 6 | |
| 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 |
|---|---|---|---|
| α-helix | 39-42 | 4 | |
| α-helix | 46-57 | 12 | |
| β-strand | 62-67 | 6 | 5 |
| α-helix | 70-72 | 3 | |
| α-helix | 73-78 | 6 | |
| α-helix | 79-85 | 7 | |
| β-strand | 96-98 | 3 | 6 |
| β-strand | 99-101 | 3 | 5 |
| β-strand | 107 | 1 | 7 |
| β-strand | 117-121 | 5 | 5 |
| β-strand | 126-131 | 6 | 6 |
| α-helix | 140-141 | 2 | |
| α-helix | 149-152 | 4 | |
| β-strand | 157 | 1 | 8 |
| α-helix | 159-166 | 8 | |
| α-helix | 169-173 | 5 | |
| α-helix | 181-186 | 6 | |
| α-helix | 191-193 | 3 | |
| β-strand | 194 | 1 | 8 |
| β-strand | 196 | 1 | 6 |
| α-helix | 199-201 | 3 | |
| α-helix | 202-205 | 4 | |
| α-helix | 207-212 | 6 | |
| β-strand | 216 | 1 | 7 |
| α-helix | 217-219 | 3 | |
| β-strand | 220-224 | 5 | 6 |
| α-helix | 227-229 | 3 | |
| β-strand | 230-235 | 6 | 5 |
| α-helix | 240-255 | 16 | |
| β-strand | 262-266 | 5 | 5 |
| β-strand | 269-273 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 46-58 | 13 | |
| β-strand | 62-67 | 6 | 9 |
| α-helix | 70-72 | 3 | |
| α-helix | 73-78 | 6 | |
| α-helix | 79-85 | 7 | |
| β-strand | 96-98 | 3 | 10 |
| β-strand | 99-101 | 3 | 9 |
| β-strand | 107 | 1 | 11 |
| β-strand | 117-121 | 5 | 9 |
| β-strand | 126-131 | 6 | 10 |
| β-strand | 157 | 1 | 12 |
| α-helix | 159-166 | 8 | |
| α-helix | 169-173 | 5 | |
| α-helix | 181-187 | 7 | |
| α-helix | 191-193 | 3 | |
| β-strand | 194 | 1 | 12 |
| β-strand | 196 | 1 | 10 |
| α-helix | 199-205 | 7 | |
| α-helix | 207-212 | 6 | |
| β-strand | 216 | 1 | 11 |
| α-helix | 217-219 | 3 | |
| β-strand | 220-224 | 5 | 10 |
| α-helix | 227-229 | 3 | |
| β-strand | 230-235 | 6 | 9 |
| α-helix | 240-255 | 16 | |
| β-strand | 262-266 | 5 | 9 |
| β-strand | 269-273 | 5 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAD(+)--protein-threonine ADP-ribosyltransferase | A, B, C | protein | 246 | Chromobacterium violaceum | Q7NY09 (AlphaFold model) |
>8UX2_1 NAD(+)--protein-threonine ADP-ribosyltransferase (chains A, B, C) GPLGSGVPHEITGGNRQEKLAQLMRQFESGGLYLRTVSDHRDEFENTFMPKLDACLGHGC DERYWSSATFIQQGLNGKVHDPHADRTGLIISADARLGGFSTFDAATANVPSGLEPSQYF PGQFPKFDMMGAYQATWNEDIFSVDATAVSEQQMDELGIPDEYRSVFDFDRIQEKMAQPR LAGREVEPTEAKICYQPKDVLGIYVDVDSPASQSKARELQQAMREQGFDLPFIAYRGGAA QELASV
Water and common crystallization additives (EDO) are not listed.
Crystal structure of bacterial ubiquitin ADP-ribosyltransferase CteC reveals a substrate-recruiting insertion. Zhang, Z., Rondon-Cordero, H.M., Das, C. J Biol Chem (2023) 300:105604-105604. DOI 10.1016/j.jbc.2023.105604 · 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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