Research workbench
Crystal structure of H5 hemagglutinin mutant (N224K, Q226L, N158D and L133A deletion) from the influenza virus A/CHICKEN/VIETNAM/NCVD- 093/2008 (H5N1)
Analyse Crystal structure of H5 hemagglutinin mutant (N224K, Q226L, N158D and L133A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E32
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin
- UniProt
- C4P282
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin | protein | 323 | 11% helix, 40% strand | C4P282 |
| B | Hemagglutinin | protein | 175 | 53% helix, 12% strand | C4P282 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.60 | 0.79 | 41 | empty |
| 2 | 66 | 0.40 | 0.80 | 14 | empty |
| 3 | 103 | 0.33 | 0.72 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2517 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 5E32 · Crystal structure of H5 hemagglutinin mutant (N224K, Q226L, N158D and L133a deletion)… · 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 C4P282
- Elsewhere: RCSB PDB 5E32 · PDBe 5E32 · UniProt C4P282
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.