MolNFT v1 · #138428 · protein
Crystal structure of murine 4-1BB N128A mutant from HEK293T cells in P43 space group
5WIW · Tumor necrosis factor receptor superfamily member 9: “Crystal structure of murine 4-1BB N128A mutant from HEK293T cells in P43 space group”. X-ray diffraction, 5 ligands (NAG, BMA, MAN). MolNFT v1 #138428 on GenesisL1: 3D structure…
- PDB
- 5WIW
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor necrosis factor receptor superfamily member 9
- UniProt
- P20334
- Ligands
- NAG, BMA, MAN, FUC, SO4
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor necrosis factor receptor superfamily member 9 | protein | 109 | 0% helix, 36% strand | P20334 |
| B | Tumor necrosis factor receptor superfamily member 9 | protein | 107 | 3% helix, 32% strand | P20334 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains B, A
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 24 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 5WIW · Crystal structure of murine 4-1BB N128A mutant from HEK293T cells in P43 space group · the same entry in another collection · chain A against A, TM-score 1.00
- P20334 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member 9… · a predicted model of the same protein · chain B against A, TM-score 0.92
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P20334
- Elsewhere: RCSB PDB 5WIW · PDBe 5WIW · UniProt P20334
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