Research workbench
Crystal structure of LI-Cadherin EC1-2
Analyse Crystal structure of LI-Cadherin EC1-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EV1
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.38
- Source
- Homo sapiens
- Molecule
- Cadherin-17
- UniProt
- Q12864
- Ligands
- CA, NA
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · resolution 1.38 · 1 distinct chain · 6% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cadherin-17 | protein | 208 | 6% helix, 44% strand | Q12864 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B
- NA · Sodium ion · metal
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.60 | 0.77 | 30 | empty |
| 2 | 199 | 0.58 | 0.80 | 39 | empty |
| 3 | 219 | 0.51 | 0.76 | 28 | empty |
| 4 | 118 | 0.41 | 0.76 | 20 | empty |
| 5 | 51 | 0.35 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 834 Ų buried · 11 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 Q12864
- Elsewhere: RCSB PDB 7EV1 · PDBe 7EV1 · UniProt Q12864
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.