MolNFT v1 · #186891 · protein
Cryo-EM structure of monomeric TTYH2
7RTV · Protein tweety homolog 2: “Cryo-EM structure of monomeric TTYH2”. Electron microscopy, 2 ligands (NAG, BMA), 3 pockets (best druggability 0.84). MolNFT v1 #186891 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7RTV
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tweety homolog 2
- UniProt
- Q3TH73
- Ligands
- NAG, BMA
- Pockets
- 3 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tweety homolog 2 | protein | 366 | 86% helix, 0% strand | Q3TH73 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.84 | 0.91 | 60 | empty |
| 2 | 760 | 0.78 | 0.81 | 56 | empty |
| 3 | 353 | 0.67 | 0.80 | 37 | empty |
Modifications
Observed in the structure: 2 disulfide, 2 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 7RTV · PDBe 7RTV · UniProt Q3TH73
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