Research workbench
Cryo-EM structure of the mal tir domain filament
Analyse Cryo-EM structure of the mal tir domain filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UZB
- Type
- protein
- Length
- 2,002 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TOLL/INTERLEUKIN-1 receptor domain-containing adapter protein
- UniProt
- P58753
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | TOLL/INTERLEUKIN-1 receptor domain-containing adapter protein | protein | 143 | 50% helix, 15% strand | P58753 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 871 | 0.72 | 0.77 | 64 | empty |
| 2 | 640 | 0.72 | 0.79 | 65 | empty |
| 3 | 920 | 0.72 | 0.76 | 64 | empty |
| 4 | 661 | 0.72 | 0.78 | 73 | empty |
| 5 | 730 | 0.71 | 0.78 | 93 | empty |
Interfaces
27 interfaces between chains.
- A–C · 589 Ų buried · 12 hydrogen bonds · protein-protein
- E–K · 584 Ų buried · 10 hydrogen bonds · protein-protein
- G–I · 583 Ų buried · 10 hydrogen bonds · protein-protein
- A–M · 577 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 538 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 5UZB · Cryo-EM structure of the MAL TIR domain filament · the same entry in another collection · chain N against N, TM-score 1.00
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 P58753
- Elsewhere: RCSB PDB 5UZB · PDBe 5UZB · UniProt P58753
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