Research workbench
Modified Form of Eosinophil-derived Neurotoxin
Analyse Modified Form of Eosinophil-derived Neurotoxin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K2A
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1
- Source
- Homo sapiens
- Molecule
- eosinophil-derived neurotoxin
- EC
- 3.1.27.5
- UniProt
- P10153
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · resolution 1 · 1 distinct chain · 23% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | eosinophil-derived neurotoxin (EC 3.1.27.5) | protein | 136 | 23% helix, 32% strand | P10153 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.43 | 0.76 | 27 | SO4 |
Modifications
Observed in the structure: 4 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 P10153
- Elsewhere: RCSB PDB 1K2A · PDBe 1K2A · UniProt P10153
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