Research workbench
Structural basis of cell-cell adhesion by cadherins
Analyse Structural basis of cell-cell adhesion by cadherins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NCH
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-cadherin
- UniProt
- P15116
- Ligands
- YB
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-cadherin | protein | 98 | 0% helix, 42% strand | P15116 |
| B | N-cadherin | protein | 100 | 4% helix, 43% strand | P15116 |
Ligands and binding sites
- YB · Ytterbium (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.74 | 0.93 | 36 | empty |
| 2 | 87 | 0.41 | 0.79 | 16 | empty |
| 3 | 54 | 0.36 | 0.79 | 14 | empty |
| 4 | 55 | 0.30 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 694 Ų buried · 4 hydrogen bonds · protein-protein
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 P15116
- Elsewhere: RCSB PDB 1NCH · PDBe 1NCH · UniProt P15116
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