Research workbench
Crystal structure of a refolded head domain hemagglutinin HA from Influenza A virus A/Fort Monmouth/1/1947
Analyse Crystal structure of a refolded head domain hemagglutinin HA from Influenza A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JP4
- Type
- protein
- Length
- 411 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Influenza A virus (A/Fort Monmouth/1/1947(H1N1))
- Molecule
- Hemagglutinin
- UniProt
- Q20MG8
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin | protein | 204 | 13% helix, 41% strand | Q20MG8 |
| B | Hemagglutinin | protein | 207 | 12% helix, 40% strand | Q20MG8 |
Ligands and binding sites
- MPO · 3[N-morpholino]propane sulfonic acid · additive · 2 copies · chains A, B
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 | 622 | 0.69 | 0.78 | 66 | empty |
| 2 | 51 | 0.34 | 0.78 | 14 | empty |
| 3 | 68 | 0.32 | 0.75 | 17 | MPO |
| 4 | 52 | 0.27 | 0.74 | 16 | MPO |
Interfaces
1 interface between chains.
- A–B · 456 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7JP4 · Crystal structure of a refolded head domain hemagglutinin ha from influenza a virus… · 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 Q20MG8
- Elsewhere: RCSB PDB 7JP4 · PDBe 7JP4 · UniProt Q20MG8
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