Research workbench
Structure of H2 japan hemagglutinin with human receptor
Analyse Structure of H2 japan hemagglutinin 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
- 2WRE
- Type
- protein
- Length
- 1,438 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin
- UniProt
- Q67085
- Ligands
- GAL, SIA
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 23% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin | protein | 471 | 24% helix, 28% strand | Q67085 |
| B | Hemagglutinin | protein | 486 | 23% helix, 31% strand | Q67085 |
| C | Hemagglutinin | protein | 481 | 23% helix, 30% strand | Q67085 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 3 copies · chains A, B, C
- SIA · N-acetyl-alpha-neuraminic acid · sugar · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.86 | 0.87 | 123 | empty |
| 2 | 116 | 0.80 | 0.98 | 21 | empty |
| 3 | 315 | 0.75 | 0.87 | 44 | empty |
| 4 | 308 | 0.72 | 0.85 | 54 | empty |
| 5 | 350 | 0.71 | 0.83 | 52 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2515 Ų buried · 34 hydrogen bonds · protein-protein
- A–C · 2454 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 2452 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
- 2WRE · structure of H2 japan hemagglutinin with human receptor · 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 Q67085
- Elsewhere: RCSB PDB 2WRE · PDBe 2WRE · UniProt Q67085
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