Research workbench
Chicken CNTN4 app complex
Analyse Chicken CNTN4 app complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MRK
- Type
- protein
- Length
- 814 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloid-beta A4 protein; Contactin-4
- UniProt
- Q9DGJ7, F1P3U6
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 4 distinct chains · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amyloid-beta A4 protein | protein | 157 | 16% helix, 38% strand | Q9DGJ7 |
| B | Contactin-4 | protein | 204 | 1% helix, 45% strand | F1P3U6 |
| C | Amyloid-beta A4 protein | protein | 155 | 16% helix, 39% strand | Q9DGJ7 |
| D | Contactin-4 | protein | 298 | 2% helix, 46% strand | F1P3U6 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 495 | 0.65 | 0.77 | 52 | empty |
| 2 | 411 | 0.60 | 0.76 | 44 | empty |
| 3 | 123 | 0.50 | 0.80 | 21 | empty |
| 4 | 105 | 0.40 | 0.76 | 20 | empty |
| 5 | 103 | 0.40 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 690 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 637 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 335 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 7MRK · Chicken CNTN4 APP complex · the same entry in another collection · chain A against A, 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 Q9DGJ7
- Every structure of UniProt F1P3U6
- Elsewhere: RCSB PDB 7MRK · PDBe 7MRK · UniProt Q9DGJ7 · UniProt F1P3U6
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