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Crystal structure of the alpha-neurexin-1 ectodomain, lns 2-6
Analyse Crystal structure of the alpha-neurexin-1 ectodomain, lns 2-6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3POY
- Type
- protein
- Length
- 1,005 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurexin-1-alpha
- UniProt
- Q28146
- Ligands
- NAG, BMA, BGC
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurexin-1-alpha | protein | 1005 | 5% helix, 46% strand | Q28146 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.75 | 0.78 | 83 | empty |
| 2 | 50 | 0.66 | 0.96 | 18 | empty |
| 3 | 110 | 0.52 | 0.82 | 23 | empty |
| 4 | 165 | 0.50 | 0.78 | 31 | empty |
| 5 | 58 | 0.41 | 0.82 | 17 | empty |
Modifications
Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation, O-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 Q28146
- Elsewhere: RCSB PDB 3POY · PDBe 3POY · UniProt Q28146
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