Solution structure of TACI-CRD2. Determined by solution NMR. Released 9 Nov 2004.
Explore 1XUT in 3D Show helices and sheets RCSB PDB PDBe
1XUT contains 1 α-helix and 2 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 |
|---|---|---|---|
| β-strand | 77-80 | 4 | 1 |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 99-102 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor receptor superfamily member 13B | A | protein | 46 | Homo sapiens | O14836 (AlphaFold model) |
>1XUT_1 Tumor necrosis factor receptor superfamily member 13B (chains A) GSPWSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLR
Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding. Hymowitz, S.G., Patel, D.R., Wallweber, H.J. et al. J Biol Chem (2005) 280:7218-7227. DOI 10.1074/jbc.M411714200 · PubMed
Other PDB entries of the same protein (UniProt O14836 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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