Crystal structure of the HAT domain of sart3. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 May 2016.
Explore 5JJX in 3D Show helices and sheets RCSB PDB PDBe
5JJX contains 18 α-helices and 0 β-strands across 1 chain. 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 | 91-107 | 17 | |
| α-helix | 112-124 | 13 | |
| α-helix | 128-141 | 14 | |
| α-helix | 146-159 | 14 | |
| α-helix | 163-176 | 14 | |
| α-helix | 183-195 | 13 | |
| α-helix | 202-217 | 16 | |
| α-helix | 225-236 | 12 | |
| α-helix | 245-255 | 11 | |
| α-helix | 262-272 | 11 | |
| α-helix | 276-278 | 3 | |
| α-helix | 279-304 | 26 | |
| α-helix | 306 | 1 | |
| α-helix | 310-323 | 14 | |
| α-helix | 326-339 | 14 | |
| α-helix | 344-354 | 11 | |
| α-helix | 361-374 | 14 | |
| α-helix | 379-392 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Squamous cell carcinoma antigen recognized by T-cells 3 | A | protein | 314 | Homo sapiens | Q15020 (AlphaFold model) |
>5JJX_1 Squamous cell carcinoma antigen recognized by T-cells 3 (chains A) GGEYEWEYDEEEEKNQLEIERLEEQLSINVYDYNCHVDLIRLLRLEGELTKVRMARQKMS EIFPLTEELWLEWLHDEISMAQDGLDREHVYDLFEKAVKDYICPNIWLEYGQYSVGGIGQ KGGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESAIVEAARLEKVHSLFRRQLAIPL YDMEATFAEYEEWSEDPIPESVIQNYNKALQQLEKYKPYEEALLQAEAPRLAEYQAYIDF EMKIGDPARIQLIFERALVENCLVPDLWIRYSQYLDRQLKVKDLVLSVHNRAIRNCPWTV ALWSRYLLAMERHG
Crystal structure of the HAT domain of sart3. ZHANG, Q., DONG, A., TEMPEL, W. et al. To be published.
Other PDB entries of the same protein (UniProt Q15020 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5JJX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.