Research workbench
Structure of the C domain of synapsin ia from bovine brain
Analyse Structure of the C domain of synapsin ia from bovine brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AUV
- Type
- protein
- Length
- 585 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synapsin ia
- UniProt
- P17599
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synapsin ia | protein | 292 | 28% helix, 33% strand | P17599 |
| B | Synapsin ia | protein | 293 | 28% helix, 31% strand | P17599 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.73 | 0.82 | 72 | empty |
| 2 | 345 | 0.72 | 0.84 | 53 | empty |
| 3 | 130 | 0.39 | 0.74 | 23 | empty |
| 4 | 61 | 0.39 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 513 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
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 P17599
- Elsewhere: RCSB PDB 1AUV · PDBe 1AUV · UniProt P17599
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