Research workbench
Crystal structure of SPINDLIN1
Analyse Crystal structure of SPINDLIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NS2
- Type
- protein
- Length
- 373 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spindlin-1
- UniProt
- Q9Y657
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spindlin-1 | protein | 201 | 6% helix, 46% strand | Q9Y657 |
| B | Spindlin-1 | protein | 172 | 3% helix, 48% strand | Q9Y657 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.46 | 0.77 | 29 | empty |
| 2 | 53 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 764 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 Q9Y657
- Elsewhere: RCSB PDB 2NS2 · PDBe 2NS2 · UniProt Q9Y657
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