Research workbench
1934 human H1 hemagglutinin
Analyse 1934 human H1 hemagglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RU7
- Type
- protein
- Length
- 2,896 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin
- UniProt
- Q82766
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Hemagglutinin | protein | 323 | 10% helix, 42% strand | Q82766 |
| B, D, H, J | Hemagglutinin | protein | 160 | 51% helix, 14% strand | Q82766 |
| F, L | Hemagglutinin | protein | 159 | 53% helix, 14% strand | Q82766 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.86 | 0.96 | 40 | empty |
| 2 | 252 | 0.84 | 0.96 | 26 | empty |
| 3 | 666 | 0.79 | 0.84 | 75 | empty |
| 4 | 596 | 0.78 | 0.84 | 75 | empty |
| 5 | 1012 | 0.76 | 0.78 | 92 | empty |
Interfaces
30 interfaces between chains.
- G–H · 2802 Ų buried · 47 hydrogen bonds · protein-protein
- C–D · 2796 Ų buried · 47 hydrogen bonds · protein-protein
- K–L · 2795 Ų buried · 48 hydrogen bonds · protein-protein
- A–B · 2785 Ų buried · 45 hydrogen bonds · protein-protein
- E–F · 2781 Ų buried · 47 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 disulfide (disulfide).
Compared structures
- 1RU7 · 1934 Human H1 Hemagglutinin · 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 Q82766
- Elsewhere: RCSB PDB 1RU7 · PDBe 1RU7 · UniProt Q82766
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