MolNFT v1 · #134455 · protein
Crystal structure of human protocadherin-15 EC3-5
5T4M: “Crystal structure of human protocadherin-15 EC3-5”. X-ray diffraction, 2 ligands (CA, CL), 4 pockets (best druggability 0.62). MolNFT v1 #134455 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T4M
- Type
- protein
- Length
- 693 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protocadherin-15
- UniProt
- Q96QU1
- Ligands
- CA, CL
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protocadherin-15 | protein | 347 | 3% helix, 41% strand | Q96QU1 |
| B | Protocadherin-15 | protein | 346 | 3% helix, 42% strand | Q96QU1 |
Ligands and binding sites
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 | 350 | 0.62 | 0.79 | 40 | empty |
| 2 | 155 | 0.46 | 0.76 | 24 | empty |
| 3 | 145 | 0.45 | 0.77 | 23 | empty |
| 4 | 54 | 0.31 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 433 Ų buried · 6 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 Q96QU1
- Elsewhere: RCSB PDB 5T4M · PDBe 5T4M · UniProt Q96QU1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.