Research workbench
Crystal structure of the soluble human 55 kd TNF receptor-human TNF- beta complex: implications for TNF receptor activation
Analyse Crystal structure of the soluble human 55 kd TNF receptor-human TNF- beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TNR
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor necrosis factor beta; Tumor necrosis factor receptor P55
- UniProt
- P01374, P19438
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor necrosis factor beta | protein | 144 | 5% helix, 57% strand | P01374 |
| R | Tumor necrosis factor receptor P55 | protein | 139 | 2% helix, 44% strand | P19438 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.48 | 0.75 | 31 | empty |
Interfaces
1 interface between chains.
- A–R · 640 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 1TNR · Crystal structure of the soluble human 55 kd TNF receptor-human TNF-beta complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P01374 · AlphaFold monomer V2.0 prediction for lymphotoxin-alpha (P01374) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P19438 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member… · a predicted model of the same protein · chain R against A, TM-score 0.96
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 P01374
- Every structure of UniProt P19438
- Elsewhere: RCSB PDB 1TNR · PDBe 1TNR · UniProt P01374 · UniProt P19438
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