Research workbench
Mouse cadherin-6 EC1-2 adhesive fragment
Analyse Mouse cadherin-6 EC1-2 adhesive fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CGU
- Type
- protein
- Length
- 828 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cadherin-6
- UniProt
- P97326
- Ligands
- CA
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cadherin-6 | protein | 207 | 1% helix, 47% strand | P97326 |
Ligands and binding sites
- CA · Calcium ion · metal · 14 copies · chains A, B, C, D
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 | 1185 | 0.78 | 0.80 | 126 | empty |
| 2 | 401 | 0.68 | 0.81 | 45 | empty |
| 3 | 74 | 0.33 | 0.75 | 16 | empty |
| 4 | 59 | 0.32 | 0.76 | 15 | empty |
| 5 | 59 | 0.31 | 0.75 | 16 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1358 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 1341 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 613 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 611 Ų buried · 8 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 P97326
- Elsewhere: RCSB PDB 6CGU · PDBe 6CGU · UniProt P97326
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