Research workbench
Crystal structure of cell adhesion molecule nectin-2/CD112 variable domain
Analyse Crystal structure of cell adhesion molecule nectin-2/CD112 variable domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DFH
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poliovirus receptor-related protein 2
- UniProt
- Q92692
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poliovirus receptor-related protein 2 | protein | 125 | 8% helix, 50% strand | Q92692 |
| B | Poliovirus receptor-related protein 2 | protein | 123 | 7% helix, 49% strand | Q92692 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.44 | 0.74 | 24 | empty |
| 2 | 75 | 0.35 | 0.76 | 16 | empty |
| 3 | 75 | 0.33 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 875 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q92692
- Elsewhere: RCSB PDB 4DFH · PDBe 4DFH · UniProt Q92692
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.