Research workbench
Solution structure of a eosinophil cationic protein-trisaccharide heparin mimetic complex
Analyse Solution structure of a eosinophil cationic protein-trisaccharide heparin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LVZ
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eosinophil cationic protein
- EC
- 3.1.27.-
- UniProt
- P12724
- Ligands
- LVZ, IDS, SGN
- Pockets
- 1 · best druggability 0.35
Structure
solution nmr · 1 distinct chain · 17% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eosinophil cationic protein (EC 3.1.27.-) | protein | 133 | 17% helix, 33% strand | P12724 |
Ligands and binding sites
- LVZ · propan-2-yl 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranoside · ligand · chains A
- IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · chains A
- SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 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 | 59 | 0.35 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2LVZ · Solution structure of a Eosinophil Cationic Protein-trisaccharide heparin mimetic complex · the same entry in another collection · chain A against A, TM-score 1.00
- P12724 · AlphaFold monomer V2.0 prediction for eosinophil cationic protein (P12724) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P12724
- Elsewhere: RCSB PDB 2LVZ · PDBe 2LVZ · UniProt P12724
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