Research workbench
Molecular basis for CD40 signaling mediated by TRAF3
Analyse Molecular basis for CD40 signaling mediated by TRAF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FLL
- Type
- protein
- Length
- 452 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TNF receptor associated factor 3; B-cell surface antigen CD40
- UniProt
- Q13114, P25942
- Pockets
- 5 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | TNF receptor associated factor 3 | protein | 205 | 23% helix, 20% strand | Q13114 |
| X, Y | B-cell surface antigen CD40 | protein | 21 | 0% helix, 0% strand | P25942 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.48 | 0.80 | 21 | empty |
| 2 | 61 | 0.32 | 0.76 | 12 | empty |
| 3 | 56 | 0.32 | 0.77 | 20 | empty |
| 4 | 68 | 0.32 | 0.75 | 20 | empty |
| 5 | 64 | 0.27 | 0.72 | 15 | empty |
Interfaces
2 interfaces between chains.
- B–Y · 651 Ų buried · 11 hydrogen bonds · protein-protein
- A–X · 633 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1FLL · Molecular basis for CD40 signaling mediated by TRAF3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q13114 · AlphaFold monomer V2.0 prediction for TNF receptor-associated factor 3 (Q13114) · a predicted model of the same protein · chain A against A, TM-score 0.94
- P25942 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member 5… · a predicted model of the same protein · chain X against A, TM-score 0.18
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 Q13114
- Every structure of UniProt P25942
- Elsewhere: RCSB PDB 1FLL · PDBe 1FLL · UniProt Q13114 · UniProt P25942
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