Research workbench
Human beta-defensin 2
Analyse Human beta-defensin 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FD3
- Type
- protein
- Length
- 162 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-defensin 2
- UniProt
- O15263
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Beta-defensin 2 | protein | 41 | 15% helix, 32% strand | O15263 |
| B, C | Beta-defensin 2 | protein | 40 | 15% helix, 30% strand | O15263 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains D
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 | 64 | 0.34 | 0.77 | 18 | empty |
Interfaces
3 interfaces between chains.
- C–D · 441 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 367 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 339 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
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 O15263
- Elsewhere: RCSB PDB 1FD3 · PDBe 1FD3 · UniProt O15263
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.