Research workbench
Modulation of agrin function by alternative splicing and CA2+ binding
Analyse Modulation of agrin function by alternative splicing and CA2+ binding in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PZ7
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agrin
- UniProt
- P31696
- Ligands
- CA
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agrin | protein | 188 | 2% helix, 46% strand | P31696 |
| B | Agrin | protein | 187 | 2% helix, 47% strand | P31696 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 111 | 0.56 | 0.84 | 25 | empty |
| 2 | 108 | 0.45 | 0.79 | 24 | empty |
| 3 | 91 | 0.44 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 174 Ų buried · 0 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 1PZ7 · PDBe 1PZ7 · UniProt P31696
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