Research workbench
Eosinophil-derived neurotoxin (edn) - adenosien-3'-5'-diphosphate complex
Analyse Eosinophil-derived neurotoxin (edn) - adenosien-3'-5'-diphosphate complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HI4
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eosinophil-derived neurotoxin
- EC
- 3.1.27.5
- UniProt
- P10153
- Ligands
- A3P
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eosinophil-derived neurotoxin (EC 3.1.27.5) | protein | 135 | 23% helix, 35% strand | P10153 |
Ligands and binding sites
- A3P · Adenosine-3'-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1HI4 · Eosinophil-derived Neurotoxin (EDN) - Adenosien-3'-5'-Diphosphate Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P10153 · AlphaFold monomer V2.0 prediction for non-secretory ribonuclease (P10153) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 1HI4 · PDBe 1HI4 · UniProt P10153
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.