Research workbench
Structure of ecp with sulphate anions at 1.50 ångströms
Analyse Structure of ecp with sulphate anions at 1.50 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OXB
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eosinophil cationic protein
- EC
- 3.1.27.-
- UniProt
- P12724
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Eosinophil cationic protein (EC 3.1.27.-) | protein | 133 | 20% helix, 32% strand | P12724 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 800 | 0.85 | 0.87 | 69 | empty |
| 2 | 118 | 0.37 | 0.74 | 20 | empty |
| 3 | 57 | 0.32 | 0.77 | 16 | empty |
| 4 | 52 | 0.28 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 755 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 P12724
- Elsewhere: RCSB PDB 4OXB · PDBe 4OXB · UniProt P12724
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