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The structure of hemagglutinin of H16 subtype influenza virus with V327G mutation
Analyse The structure of hemagglutinin of H16 subtype influenza virus with V327G… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FIU
- Type
- protein
- Length
- 1,527 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin
- UniProt
- Q5DL24
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Hemagglutinin | protein | 509 | 26% helix, 32% strand | Q5DL24 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.86 | 0.96 | 39 | empty |
| 2 | 783 | 0.80 | 0.84 | 94 | empty |
| 3 | 572 | 0.70 | 0.79 | 53 | empty |
| 4 | 429 | 0.69 | 0.81 | 48 | empty |
| 5 | 271 | 0.64 | 0.81 | 25 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2452 Ų buried · 41 hydrogen bonds · protein-protein
- A–C · 2439 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 2403 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 4FIU · The structure of hemagglutinin of H16 subtype influenza virus with V327G mutation · 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 Q5DL24
- Elsewhere: RCSB PDB 4FIU · PDBe 4FIU · UniProt Q5DL24
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