Research workbench
Structure of the parainfluenza virus 5 (PIV5) hemagglutinin- neuraminidase (hn) stalk domain
Analyse Structure of the parainfluenza virus 5 (PIV5) hemagglutinin- neuraminidase (hn)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TSI
- Type
- protein
- Length
- 199 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin-neuraminidase
- EC
- 3.2.1.18
- UniProt
- P04850
Structure
x-ray diffraction · 3 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemagglutinin-neuraminidase (EC 3.2.1.18) | protein | 50 | 88% helix, 0% strand | P04850 |
| B | Hemagglutinin-neuraminidase (EC 3.2.1.18) | protein | 48 | 94% helix, 0% strand | P04850 |
| D | Hemagglutinin-neuraminidase (EC 3.2.1.18) | protein | 51 | 86% helix, 0% strand | P04850 |
Interfaces
6 interfaces between chains.
- A–B · 1001 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 996 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 966 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 881 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 105 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3TSI · Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) stalk… · the same entry in another collection · chain A against A, TM-score 1.00
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 P04850
- Elsewhere: RCSB PDB 3TSI · PDBe 3TSI · UniProt P04850
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.