MolNFT v1 · #18764 · protein
Modulation of agrin function by alternative splicing and CA2+ binding
1PZ9: “Modulation of agrin function by alternative splicing and CA2+ binding”. X-ray diffraction, 3 pockets (best druggability 0.65). MolNFT v1 #18764 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PZ9
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agrin
- UniProt
- P31696
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agrin | protein | 185 | 4% helix, 43% strand | P31696 |
| B | Agrin | protein | 187 | 2% helix, 43% strand | P31696 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.65 | 0.77 | 54 | empty |
| 2 | 143 | 0.47 | 0.77 | 27 | empty |
| 3 | 58 | 0.43 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 347 Ų buried · 3 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 P31696
- Elsewhere: RCSB PDB 1PZ9 · PDBe 1PZ9 · UniProt P31696
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