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Crystal structure of aaa of spastin
Analyse Crystal structure of aaa of spastin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z6Q
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spastin
- EC
- 3.6.4.3
- UniProt
- Q9UBP0
- Ligands
- CL
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spastin (EC 3.6.4.3) | protein | 272 | 49% helix, 11% strand | Q9UBP0 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.59 | 0.82 | 30 | empty |
| 2 | 173 | 0.58 | 0.81 | 28 | empty |
| 3 | 150 | 0.51 | 0.79 | 26 | empty |
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 Q9UBP0
- Elsewhere: RCSB PDB 5Z6Q · PDBe 5Z6Q · UniProt Q9UBP0
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