Research workbench
Crystal structure of human beta-defensin 4 (HBD4)
Analyse Crystal structure of human beta-defensin 4 (HBD4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KI9
- Type
- protein
- Length
- 43 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-defensin 104
- UniProt
- Q8WTQ1
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-defensin 104 | protein | 43 | 7% helix, 40% strand | Q8WTQ1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 3 modified (disulfide, methylation).
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 Q8WTQ1
- Elsewhere: RCSB PDB 5KI9 · PDBe 5KI9 · UniProt Q8WTQ1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.