Research workbench
Crystal structure of mouse protocadherin-15 EC5-7 I582T
Analyse Crystal structure of mouse protocadherin-15 EC5-7 I582T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BXU
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protocadherin-15
- UniProt
- Q99PJ1
- Ligands
- CA
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protocadherin-15 | protein | 312 | 2% helix, 44% strand | Q99PJ1 |
| B | Protocadherin-15 | protein | 311 | 3% helix, 44% strand | Q99PJ1 |
Ligands and binding sites
- CA · Calcium ion · metal · 10 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.60 | 0.80 | 40 | empty |
| 2 | 280 | 0.59 | 0.78 | 29 | empty |
| 3 | 197 | 0.53 | 0.78 | 31 | empty |
| 4 | 53 | 0.24 | 0.72 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1095 Ų buried · 12 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 Q99PJ1
- Elsewhere: RCSB PDB 6BXU · PDBe 6BXU · UniProt Q99PJ1
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