Research workbench
Crystal structure of monomeric variant of human alpha-defensin 5, HD5 (GLU21EME mutant)
Analyse Crystal structure of monomeric variant of human alpha-defensin 5, HD5 (GLU21EME… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E82
- Type
- protein
- Length
- 62 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Defensin-5
- UniProt
- Q01523
- Ligands
- EME
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Defensin-5 | protein | 31 | 0% helix, 42% strand | Q01523 |
Ligands and binding sites
- EME · N-methyl-L-glutamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 267 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 covalent (disulfide, covalent ligand).
Compared structures
- 4E82 · Crystal structure of monomeric variant of human alpha-defensin 5, HD5 (Glu21EMe mutant) · the same entry in another collection · chain A against A, TM-score 1.00
- Q01523 · AlphaFold monomer V2.0 prediction for defensin-5 (Q01523) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 4E82 · PDBe 4E82 · UniProt Q01523
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