Research workbench
Human H7N9 influenza virus haemagglutinin in complex with human receptor analogue lstc
Analyse Human H7N9 influenza virus haemagglutinin in complex with human receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BSE
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haemagglutinin HA1; Haemagglutinin HA2
- UniProt
- M4YV75
- Ligands
- NAG, GAL, SIA, SO4
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Haemagglutinin HA1 | protein | 316 | 9% helix, 39% strand | M4YV75 |
| B | Haemagglutinin HA2 | protein | 170 | 56% helix, 13% strand | M4YV75 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · chains A
- SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A
- SO4 · Sulfate ion · ion · 15 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.64 | 0.83 | 26 | empty |
| 2 | 110 | 0.48 | 0.80 | 21 | SO4 |
Interfaces
1 interface between chains.
- A–B · 3188 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 4BSE · Human H7N9 Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue LSTc · 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 M4YV75
- Elsewhere: RCSB PDB 4BSE · PDBe 4BSE · UniProt M4YV75
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