Research workbench
Structure of ecp in complex with citrate ions at 1.50 ångströms
Analyse Structure of ecp in complex with citrate ions 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
- 4OXF
- Type
- protein
- Length
- 267 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
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eosinophil cationic protein (EC 3.1.27.-) | protein | 134 | 19% helix, 33% strand | P12724 |
| B | Eosinophil cationic protein (EC 3.1.27.-) | protein | 133 | 18% helix, 34% strand | P12724 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- CIT · Citric acid · additive · 5 copies · chains A, B
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 | 174 | 0.43 | 0.74 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 4OXF · Structure of ECP in complex with citrate ions at 1.50 Angstroms · 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 B against A, TM-score 0.98
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 4OXF · PDBe 4OXF · UniProt P12724
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