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The crystal structure of hemagglutinin from A/PORT CHALMERS/1/1973 influenza virus
Analyse The crystal structure of hemagglutinin from A/PORT CHALMERS/1/1973 influenza… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WE5
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
- UniProt
- Q1PUD9
- Ligands
- NAG, BMA
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin HA1 chain | protein | 321 | 11% helix, 39% strand | Q1PUD9 |
| B | Hemagglutinin HA2 chain | protein | 172 | 53% helix, 14% strand | Q1PUD9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.55 | 0.90 | 17 | empty |
| 2 | 188 | 0.54 | 0.79 | 36 | empty |
| 3 | 64 | 0.33 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2987 Ų buried · 49 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 4WE5 · The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus · 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 Q1PUD9
- Elsewhere: RCSB PDB 4WE5 · PDBe 4WE5 · UniProt Q1PUD9
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