Research workbench
Cryo-EM structure of a TTYH2 trans-dimer
Analyse Cryo-EM structure of a TTYH2 trans-dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RTU
- Type
- protein
- Length
- 754 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tweety homolog 2
- UniProt
- Q3TH73
- Ligands
- NAG, BMA
- Pockets
- 7 · best druggability 0.78
Structure
electron microscopy · 2 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tweety homolog 2 | protein | 395 | 81% helix, 1% strand | Q3TH73 |
| B | Protein tweety homolog 2 | protein | 359 | 88% helix, 0% strand | Q3TH73 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 4 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.78 | 0.83 | 51 | empty |
| 2 | 578 | 0.78 | 0.84 | 52 | empty |
| 3 | 488 | 0.74 | 0.83 | 44 | empty |
| 4 | 149 | 0.61 | 0.84 | 22 | empty |
| 5 | 141 | 0.42 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 925 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
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 Q3TH73
- Elsewhere: RCSB PDB 7RTU · PDBe 7RTU · UniProt Q3TH73
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