MolNFT v1 · #129397 · protein
Crystal structure of the chicken MDGA1 ectodomain in complex with the human neuroligin 1 (NL1(-a-B)) cholinesterase domain.
5OJ6: “Crystal structure of the chicken MDGA1 ectodomain in complex with the human neuroligin 1 (NL1(-a-B))…”. X-ray diffraction, 2 ligands (NAG, BMA). MolNFT v1 #129397 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OJ6
- Type
- protein
- Length
- 1,236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8N2Q7, Q0WYX8
- Ligands
- NAG, BMA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 547 | — | Q8N2Q7 |
| B | — | protein | 689 | — | Q0WYX8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains B
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OJ6 · Crystal structure of the chicken MDGA1 ectodomain in complex with the human neuroligin 1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8N2Q7 · AlphaFold monomer V2.0 prediction for neuroligin-1 (Q8N2Q7) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q0WYX8 · AlphaFold monomer V2.0 prediction for mam domain-containing glycosylphosphatidylinositol… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q8N2Q7
- Every structure of UniProt Q0WYX8
- Elsewhere: RCSB PDB 5OJ6 · PDBe 5OJ6 · UniProt Q8N2Q7 · UniProt Q0WYX8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.