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The crystal structure of hemagglutinin from A/CANINE/IL/11613/2015 (H3N2) influenza virus.
Analyse The crystal structure of hemagglutinin from A/CANINE/IL/11613/2015 (H3N2)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N4F
- Type
- protein
- Length
- 1,956 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1; Hemagglutinin HA2
- UniProt
- A0A218KIQ1, A0A2U5FPI7
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Hemagglutinin HA1 | protein | 317 | 10% helix, 38% strand | A0A218KIQ1 |
| B, D, F, H | Hemagglutinin HA2 | protein | 172 | 48% helix, 11% strand | A0A2U5FPI7 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 905 | 0.86 | 0.88 | 106 | empty |
| 2 | 216 | 0.83 | 0.95 | 29 | empty |
| 3 | 990 | 0.74 | 0.78 | 108 | empty |
| 4 | 88 | 0.72 | 0.96 | 22 | empty |
| 5 | 444 | 0.70 | 0.81 | 52 | empty |
Interfaces
17 interfaces between chains.
- E–F · 2903 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 2900 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2895 Ų buried · 41 hydrogen bonds · protein-protein
- G–H · 2891 Ų buried · 39 hydrogen bonds · protein-protein
- B–D · 1439 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide (disulfide).
Compared structures
- 6N4F · The crystal structure of hemagglutinin from A/canine/IL/11613/2015 (H3N2) 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 A0A218KIQ1
- Every structure of UniProt A0A2U5FPI7
- Elsewhere: RCSB PDB 6N4F · PDBe 6N4F · UniProt A0A218KIQ1 · UniProt A0A2U5FPI7
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