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Crystal structure of defensin hnp-3, an amphiphilic dimer: mechanisms of membrane permeabilization
Analyse Crystal structure of defensin hnp-3, an amphiphilic dimer: mechanisms of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DFN
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Defensin hnp-3
- UniProt
- P59665
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Defensin hnp-3 | protein | 30 | 0% helix, 53% strand | P59665 |
Interfaces
1 interface between chains.
- A–B · 450 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1DFN · Crystal structure of defensin hnp-3, an amphiphilic dimer: mechanisms of membrane… · the same entry in another collection · chain A against A, TM-score 1.00
- P59665 · AlphaFold monomer V2.0 prediction for neutrophil defensin 1 (P59665) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P59665
- Elsewhere: RCSB PDB 1DFN · PDBe 1DFN · UniProt P59665
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