Research workbench
Crystal structure of human alpha-defensin 5, HD5 (LEU29NLE mutant)
Analyse Crystal structure of human alpha-defensin 5, HD5 (LEU29NLE mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E83
- Type
- protein
- Length
- 64 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Defensin-5
- UniProt
- Q01523
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Defensin-5 | protein | 32 | 0% helix, 59% strand | Q01523 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 modified (disulfide, nonstandard).
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 Q01523
- Elsewhere: RCSB PDB 4E83 · PDBe 4E83 · UniProt Q01523
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