Research workbench
Human teneurin-2 and human latrophilin-3 binary complex
Analyse Human teneurin-2 and human latrophilin-3 binary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VHH
- Type
- protein
- Length
- 1,821 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NT68, Q9HAR2
- Ligands
- NAG, MAN, BMA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1723 | — | Q9NT68 |
| B | — | protein | 98 | — | Q9HAR2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VHH · Human Teneurin-2 and human Latrophilin-3 binary complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HAR2 · AlphaFold monomer V2.0 prediction for adhesion G protein-coupled receptor L3 (Q9HAR2) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q9NT68
- Every structure of UniProt Q9HAR2
- Elsewhere: RCSB PDB 6VHH · PDBe 6VHH · UniProt Q9NT68 · UniProt Q9HAR2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.