1XU2: APRIL
The crystal structure of APRIL bound to BCMA. Determined by X-ray diffraction at 2.35 Å resolution. Released 9 Nov 2004.
- Method
- X-ray diffraction
- Resolution
- 2.35 Å
- Organisms
- Mus musculus, Homo sapiens
- Chains
- 6
- Atoms
- 4,119
- Mol. weight
- 62.08 kDa
- Ligands
- NI
- Released
- 9 Nov 2004
Explore 1XU2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1XU2 contains 8 α-helices and 39 β-strands across 6 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.
Chain A: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 108-117 | 10 | 1 |
| β-strand | 125-135 | 11 | 1 |
| β-strand | 139-142 | 4 | 1 |
| β-strand | 145-148 | 4 | 1 |
| β-strand | 152-163 | 12 | 1 |
| β-strand | 168-176 | 9 | 1 |
| β-strand | 181-190 | 10 | 1 |
| α-helix | 195-197 | 3 | |
| β-strand | 199-210 | 12 | 1 |
| β-strand | 215-220 | 6 | 1 |
| β-strand | 227 | 1 | 1 |
| β-strand | 235-240 | 6 | 1 |
Chain B: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 108-117 | 10 | 2 |
| β-strand | 125-135 | 11 | 2 |
| β-strand | 139-142 | 4 | 2 |
| β-strand | 145-148 | 4 | 2 |
| β-strand | 152-162 | 11 | 2 |
| β-strand | 168-176 | 9 | 2 |
| β-strand | 181-190 | 10 | 2 |
| β-strand | 200-210 | 11 | 2 |
| α-helix | 211 | 1 | |
| β-strand | 215-220 | 6 | 2 |
| β-strand | 227 | 1 | 2 |
| β-strand | 235-240 | 6 | 2 |
Chain D: 0 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 108-117 | 10 | 3 |
| β-strand | 125-135 | 11 | 3 |
| β-strand | 139-142 | 4 | 3 |
| β-strand | 145-148 | 4 | 3 |
| β-strand | 152-163 | 12 | 3 |
| β-strand | 168-176 | 9 | 3 |
| β-strand | 181-190 | 10 | 3 |
| β-strand | 199-210 | 12 | 3 |
| β-strand | 215-220 | 6 | 3 |
| β-strand | 227 | 1 | 3 |
| β-strand | 235-240 | 6 | 3 |
Chain R: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 4 |
| β-strand | 20-23 | 4 | 4 |
| α-helix | 24-26 | 3 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-42 | 5 | |
Chain S: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 5 |
| β-strand | 20-23 | 4 | 5 |
| α-helix | 24-27 | 4 | |
| α-helix | 38-41 | 4 | |
Chain T: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-15 | 4 | 6 |
| β-strand | 20-23 | 4 | 6 |
| α-helix | 24-27 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tumor necrosis factor ligand superfamily member 13 | A, B, D | protein | 138 | Mus musculus | Q9D777 (AlphaFold model) |
| Tumor necrosis factor receptor superfamily member 17 | R, S, T | protein | 47 | Homo sapiens | Q02223 (AlphaFold model) |
Sequence of entity 1 (A, B, D), FASTA
>1XU2_1 Tumor necrosis factor ligand superfamily member 13 (chains A, B, D)
KKHSVLHLVPVNITSKADSDVTEVMWQPVLRRGRGLEAQGDIVRVWDTGIYLLYSQVLFH
DVTFTMGQVVSREGQGRRETLFRCIRSMPSDPDRAYNSCYSAGVFHLHQGDIITVKIPRA
NAKLSLSPHGTFLGFVKL
Sequence of entity 2 (R, S, T), FASTA
>1XU2_2 Tumor necrosis factor receptor superfamily member 17 (chains R, S, T)
AGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NI | Nickel (II) ion | Ni | 1 |
Primary citation
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.A. et al. J Biol Chem (2005) 280:7218-7227. DOI 10.1074/jbc.M411714200 · PubMed
Other PDB entries of the same protein (UniProt Q9D777 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1U5X 1.8 Å, Crystal structure of murine APRIL at pH 5.0
- 1XU1 1.9 Å, The crystal structure of APRIL bound to TACI
- 1U5Y 2.3 Å, Crystal structure of murine APRIL, pH 8.0
- 1U5Z 2.4 Å, The Crystal structure of murine APRIL, pH 8.5
- 3K48 2.8 Å, Crystal structure of APRIL bound to a peptide
Browse structure collections
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