Research workbench
Crystal structure of the A/BRISBANE/10/2007 (H3N2) influenza virus hemagglutinin L194P mutant apo form
Analyse Crystal structure of the A/BRISBANE/10/2007 (H3N2) influenza virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AOP
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
- UniProt
- I6UCL3, A8W891
- Ligands
- NAG, BMA, MAN
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin HA1 chain | protein | 317 | 9% helix, 41% strand | I6UCL3 |
| B | Hemagglutinin HA2 chain | protein | 173 | 50% helix, 16% strand | A8W891 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
- MAN · alpha-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.57 | 0.91 | 17 | empty |
| 2 | 103 | 0.39 | 0.76 | 19 | empty |
| 3 | 75 | 0.33 | 0.75 | 16 | empty |
| 4 | 57 | 0.28 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3077 Ų buried · 44 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 glycan, 6 disulfide (N-glycosylation, disulfide).
Compared structures
- 6AOP · Crystal structure of the A/Brisbane/10/2007 (H3N2) influenza virus hemagglutinin L194P… · 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 I6UCL3
- Every structure of UniProt A8W891
- Elsewhere: RCSB PDB 6AOP · PDBe 6AOP · UniProt I6UCL3 · UniProt A8W891
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