Research workbench
Chicken CNTN3 app complex
Analyse Chicken CNTN3 app complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MRM
- Type
- protein
- Length
- 725 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion protein of chicken CNTN3 FN1-FN2 domains and amyloid-beta A4 PROTEIN,AMYLOID-beta…
- UniProt
- F1NL84, Q9DGJ7
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Fusion protein of chicken CNTN3 FN1-FN2 domains and amyloid-beta A4 PROTEIN,AMYLOID-beta A4 protein | protein | 360 | 8% helix, 40% strand | F1NL84, Q9DGJ7 |
| A | Fusion protein of chicken CNTN3 FN1-FN2 domains and amyloid-beta A4 PROTEIN,AMYLOID-beta A4 protein | protein | 365 | 8% helix, 39% strand | F1NL84, Q9DGJ7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 494 | 0.61 | 0.75 | 41 | empty |
| 2 | 327 | 0.57 | 0.76 | 33 | empty |
| 3 | 92 | 0.39 | 0.76 | 17 | empty |
| 4 | 132 | 0.37 | 0.72 | 25 | empty |
| 5 | 77 | 0.35 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- B–A · 845 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 7MRM · Chicken CNTN3 APP complex · the same entry in another collection · chain B against B, TM-score 1.00
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 F1NL84
- Every structure of UniProt Q9DGJ7
- Elsewhere: RCSB PDB 7MRM · PDBe 7MRM · UniProt F1NL84 · UniProt Q9DGJ7
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