MolNFT v1 · #102808 · protein
Structure of ECP/H15A mutant.
4OWZ · Eosinophil cationic protein: “Structure of ECP/H15A mutant.”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.43). MolNFT v1 #102808 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4OWZ
- Type
- protein
- Length
- 268 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
- FE
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Eosinophil cationic protein (EC 3.1.27.-) | protein | 134 | 18% helix, 33% strand | P12724 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- CIT · Citric acid · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.43 | 0.78 | 17 | empty |
| 2 | 127 | 0.41 | 0.75 | 25 | empty |
| 3 | 84 | 0.39 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 487 Ų buried · 3 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 4OWZ · PDBe 4OWZ · UniProt P12724
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